ID   ARGI_SOYBN              Reviewed;         350 AA.
AC   O49046;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Arginase;
DE            EC=3.5.3.1 {ECO:0000250|UniProtKB:P05089};
GN   Name=AG1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Williams 82;
RA   Goldraij A., Coello P., Polacco J.C.;
RT   "Nucleotide sequence of a cDNA encoding a soybean seedling axes arginase.";
RL   (er) Plant Gene Register PGR98-016(1998).
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   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00742}.
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DR   EMBL; AF035671; AAC04613.1; -; mRNA.
DR   PIR; T06222; T06222.
DR   RefSeq; NP_001237121.1; NM_001250192.1.
DR   AlphaFoldDB; O49046; -.
DR   SMR; O49046; -.
DR   STRING; 3847.GLYMA03G03270.1; -.
DR   PRIDE; O49046; -.
DR   GeneID; 547994; -.
DR   KEGG; gmx:547994; -.
DR   eggNOG; KOG2964; Eukaryota.
DR   InParanoid; O49046; -.
DR   OrthoDB; 921352at2759; -.
DR   UniPathway; UPA00158; UER00270.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
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, using agmatinase; IBA:GO_Central.
DR   GO; GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR11358; PTHR11358; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   SUPFAM; SSF52768; SSF52768; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Arginine metabolism; Hydrolase; Manganese; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..350
FT                   /note="Arginase"
FT                   /id="PRO_0000173705"
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         193
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         195..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         195
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         197
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         203..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         278
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         280
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P53608"
SQ   SEQUENCE   350 AA;  38610 MW;  856CF5BADC5A15D4 CRC64;
     MSFLRSFARN KDISKVGRRG IHCMQKLCAE KISPDSLEKA QNRVIDAALT LVRENTGLRK
     NLCHSLGGAV ATSTLLGVPL GHNSSFLEGP AFAPPFIREG IWCGSANSTT EEGKDLKDLR
     IMVDVGDIPI QEMRDCGIGD ERLMKVVSDS VKLVMEEDPL RPLILGGDPS ISYPVVRAIS
     EKLGGPVDVL HFDAHPDLYD EFEGNYYSHA SSFARIMEGG YARRLLQVGI RSINKEGREQ
     AKKFGVEQFE MRHFSKDRPF LENLNLGEGA KGVYISIDVD CLDPGYAVGV SHYESGGLSF
     RDVMNMLQNL KGDIVGGDVV EYNPQREPPD RMTAMVAAKF VRELAAKMSK