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Database: UniProt
Entry: A0A4Q1B9T7_TREME
LinkDB: A0A4Q1B9T7_TREME
Original site: A0A4Q1B9T7_TREME 
ID   A0A4Q1B9T7_TREME        Unreviewed;       352 AA.
AC   A0A4Q1B9T7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   28-JAN-2026, entry version 25.
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=M231_07180 {ECO:0000313|EMBL:RXK35548.1};
OS   Tremella mesenterica (Jelly fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Tremellaceae; Tremella.
OX   NCBI_TaxID=5217 {ECO:0000313|EMBL:RXK35548.1, ECO:0000313|Proteomes:UP000289152};
RN   [1] {ECO:0000313|EMBL:RXK35548.1, ECO:0000313|Proteomes:UP000289152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28783 {ECO:0000313|EMBL:RXK35548.1,
RC   ECO:0000313|Proteomes:UP000289152};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361159};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR036979-1,
CC         ECO:0000256|RuleBase:RU361159};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR036979-1, 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:RXK35548.1}.
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DR   EMBL; SDIL01000131; RXK35548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q1B9T7; -.
DR   FunCoup; A0A4Q1B9T7; 301.
DR   STRING; 5217.A0A4Q1B9T7; -.
DR   VEuPathDB; FungiDB:TREMEDRAFT_44779; -.
DR   InParanoid; A0A4Q1B9T7; -.
DR   OMA; YKEFRYA; -.
DR   OrthoDB; 9992747at2759; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000289152; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:TreeGrafter.
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|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR036979-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR036979-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289152}.
FT   BINDING         147
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         174
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         276
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
SQ   SEQUENCE   352 AA;  37492 MW;  688BDC26B7B1B289 CRC64;
     MSPGYEFKFL SKPATVAIVG CPFSGGQGKA GVDLAPNALV SAGLIDQLFN LGWEVHYESE
     LHFSEIPYNP APPHVLGAAI HEQVEVNVPV NSSPQAKKAT MIQKLPDPDI GKMKKPRLVS
     AVCEKVSKEV GEIAGKGWLP LTLGGDHSLA MGTVSGTKSK YPDACLIWID AHADINTPET
     TDSGNLHGCP VSFLLGLTGT AVEPFSTWLK PCLKPSELVY IGLRDIDAPE RAILRENGIK
     AFSMHEVDKY GIGKVVEMAL DHVNPKRDKP VHLSFDVDAL DPDVAPSTGT PVRGGLTFRE
     GHYITEAIAE TGLLVSLDIM EVNPSLLDSS AVSQTIAVGC SLTRAALGET LL
//
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