ARGI_ASHGO
ID ARGI_ASHGO Reviewed; 399 AA.
AC Q74ZW4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Arginase;
DE EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN Name=CAR1; OrderedLocusNames=AGR225C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; AE016820; AAS54715.1; -; Genomic_DNA.
DR RefSeq; NP_986891.1; NM_211953.1.
DR AlphaFoldDB; Q74ZW4; -.
DR SMR; Q74ZW4; -.
DR STRING; 33169.AAS54715; -.
DR PRIDE; Q74ZW4; -.
DR EnsemblFungi; AAS54715; AAS54715; AGOS_AGR225C.
DR GeneID; 4623193; -.
DR KEGG; ago:AGOS_AGR225C; -.
DR eggNOG; KOG2965; Eukaryota.
DR HOGENOM; CLU_039478_6_1_1; -.
DR InParanoid; Q74ZW4; -.
DR OMA; IATCFGQ; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1903269; C:ornithine carbamoyltransferase inhibitor complex; IEA:EnsemblFungi.
DR GO; GO:0004053; F:arginase activity; IBA:GO_Central.
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: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 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Hydrolase; Manganese; Metal-binding;
KW Reference proteome; Urea cycle.
FT CHAIN 1..399
FT /note="Arginase"
FT /id="PRO_0000173706"
FT BINDING 193
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 218..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 220
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 229..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 324
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53608"
SQ SEQUENCE 399 AA; 42555 MW; 8DDCF23F497F51EB CRC64;
MAQRNCWRRS WLGVGGGLCL GAHGAARGPR QLFHLTAKQS SAASDAKCRR WRAAGRGGGA
GGVYNGRGAA AGSRQTSGMA HNEHPHYKFF ESKKASLVMA PFSGGQGKSG VEDGPKYLLK
QGLREGVEGL GWEIEVQRPL DGHDFEERKQ RATEVVGRAK NPTLVGEATH LIHDAVRAAA
HAGRLPVTLG GDHSIAIGTV SGVLDRYPDA GLLWVDAHAD INTLASTESG NLHGCPVSFL
MGLERESWPA PLAWVPGTLR PSKIAYIGLR DVDPEEKEIL RRLGITAFSM YHVDRYGINK
VVEMALAAIN PDGTGPVMVS YDVDAIDPMY VPATGTPVRG GLTLREGLFI VERVAETGNL
VALDVVECNP ELAAHDLHVV DTVQTGCSIA RCALGETLL
