ID A0A371DV90_9APHY Unreviewed; 317 AA.
AC A0A371DV90;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=OH76DRAFT_1395547 {ECO:0000313|EMBL:RDX56431.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX56431.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX56431.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX56431.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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}.
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DR EMBL; KZ857380; RDX56431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DV90; -.
DR STRING; 139420.A0A371DV90; -.
DR UniPathway; UPA00158; UER00270.
DR Proteomes; UP000256964; 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 PIRSF; PIRSF036979; 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:UP000256964}.
SQ SEQUENCE 317 AA; 34173 MW; 58A0711090BE6102 CRC64;
MASHLESSVS RFLPDPKTVA IVGCPFRGGQ AKLGVDNGPI HLVEAGLPEQ LAELGWQVKF
DGHHQFATID AENDPPIGKL KNPRFVSRVC KSVAEVVGDH AKKGQLPLTL GGDHSLAMGT
ISGTLEKYPD ACVIWVDAHA DINTAETTDS GNIHGMPLSF LLGIGPKVDE FSWVKPVLKP
HRLVYIGLRD VDQGERRILK EHGIKAFSMH EVDKYGIGRV VEMALDHVNP GRKLPIHLSF
DVDALDPTVA PSTGTPVRGG LTFREGHYIC ESVYETGCLV ALDIMEVNPS LADEESVKQT
VAVGCSLARS ALGETLL
//
