ID A0A397HUL4_9EURO Unreviewed; 324 AA.
AC A0A397HUL4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Arginase {ECO:0000256|ARBA:ARBA00018123, ECO:0000256|RuleBase:RU361159};
DE EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168, ECO:0000256|RuleBase:RU361159};
GN ORFNames=CDV56_109126 {ECO:0000313|EMBL:RHZ66905.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ66905.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ66905.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ66905.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000227,
CC ECO:0000256|RuleBase:RU361159};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU361159};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|RuleBase:RU361159};
CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-
CC arginine: step 1/1. {ECO:0000256|ARBA:ARBA00005098}.
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ66905.1}.
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DR EMBL; NKHU02000009; RHZ66905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HUL4; -.
DR STRING; 41047.A0A397HUL4; -.
DR VEuPathDB; FungiDB:CDV56_109126; -.
DR OrthoDB; 161483at2759; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000215305; Unassembled WGS sequence.
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 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 {ECO:0000256|ARBA:ARBA00022503,
KW ECO:0000256|RuleBase:RU361159};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW Manganese {ECO:0000256|RuleBase:RU361159};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361159};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305}.
SQ SEQUENCE 324 AA; 35433 MW; 9DE1A0780D717D4B CRC64;
MTSPSTIKQR FLTKPNELGV VAVGFNGGQC KLGVEAAPLA LIEAGLLNQV RDDLGYEVHY
DDTVHYYENL TPLSDPDHRG MKKPRAVSVV TETLSKQVYD HAKDGKFVLT LGGDHSIAIG
TISGTAKAIR ERLGREMAVI WVDAHADLNT PEMSPSGNIH GMPMAFLTRL AQEDKKDIFG
WLEDEHIINK NKLVYIGLRD VDRGEKQLLR EHGIKAFSMH DIDRHGIGRV VEMALAHIGN
DTPIHLSFDV DALDPQWAPS TGTPVRGGLT LREGDFICEC VHETGNLVAM DLVEVNPSLE
EVGASETIRA GCSLVRCALG DTLL
//
