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Database: UniProt
Entry: A0A6G1BZV1_9ORYZ
LinkDB: A0A6G1BZV1_9ORYZ
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ID   A0A6G1BZV1_9ORYZ        Unreviewed;       484 AA.
AC   A0A6G1BZV1;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   28-JAN-2026, entry version 18.
DE   RecName: Full=Arginase 1, mitochondrial {ECO:0000256|ARBA:ARBA00071872};
DE            EC=3.5.3.1 {ECO:0000256|ARBA:ARBA00012168};
DE   AltName: Full=Arginine amidohydrolase 1 {ECO:0000256|ARBA:ARBA00078159};
GN   ORFNames=E2562_023490 {ECO:0000313|EMBL:KAF0893237.1};
OS   Oryza meyeriana var. granulata.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza meyeriana.
OX   NCBI_TaxID=110450 {ECO:0000313|EMBL:KAF0893237.1, ECO:0000313|Proteomes:UP000479710};
RN   [1] {ECO:0000313|EMBL:KAF0893237.1, ECO:0000313|Proteomes:UP000479710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Menghai {ECO:0000313|Proteomes:UP000479710};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF0893237.1};
RA   Li W.;
RT   "Whole genome sequence of Oryza granulata.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of L-arginine to urea and L-
CC       ornithine. The latter can be utilized in the urea cycle or as a
CC       precursor for the synthesis of both polyamines and proline.
CC       {ECO:0000256|ARBA:ARBA00058137}.
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|ARBA:ARBA00047391};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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. Agmatinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009227}.
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:KAF0893237.1}.
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DR   EMBL; SPHZ02000011; KAF0893237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6G1BZV1; -.
DR   OrthoDB; 288726at2759; -.
DR   Proteomes; UP000479710; Unassembled WGS sequence.
DR   GO; GO:0008783; F:agmatinase activity; IEA:TreeGrafter.
DR   GO; GO:0004053; F:arginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033389; P:putrescine biosynthetic process from arginine, via agmatine; IEA:TreeGrafter.
DR   CDD; cd11593; Agmatinase-like_2; 1.
DR   FunFam; 3.40.800.10:FF:000007; Arginase 1, mitochondrial; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   PANTHER; PTHR11358:SF26; GUANIDINO ACID HYDROLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00491; Arginase; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000479710}.
FT   REGION          73..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..85
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   484 AA;  52516 MW;  E517DEBB911B6257 CRC64;
     MGGVAAGTKW IHHVRRLSAA KVSSDALERG QSRVIDASLT LIRERAKLKV SIFTPFPPFP
     FFLPPLTVPP VPLRPTPNSS PPCCPDAPDS TTPHPHPRCH ATPQLPHRRW PLVFPGAGRS
     SAALPGATPT RLRRPWPPFG AAFFADGLPQ RPAPAAPVQP SPALYRAVPT RLISPPPPAC
     NIVMENYYYV PVSAELLRAL GGVKASACLL GVPLGHNSSF LQGPAFAPPR IREAIWCGST
     NSSTEEGKEL NDPRVLTDVG DVPIQEIRDC GVEDNRLMNV VSESVKTVME EDPLRPLVLG
     GDHSISYPVV RAVSEKLGGP VDILHLDAHP DIYDAFEGNI YSHASSFARI MEGGYARRLL
     QVGIRSITKE GREQGKRFGV EQYEMRTFSK DREKLESLKL GEGVKGVYIS VDVDCLDPAF
     APGVSHIEPG GLSFRDVLNI LHNLQGDVVA GDVVEFNPQR DTVDGMTAMV AAKLVRELTA
     RISK
//
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