ID ARGI_MEDTR Reviewed; 338 AA. AC G7JFU5; A0A0C3WTP8; DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2014, sequence version 2. DT 14-DEC-2022, entry version 60. DE RecName: Full=Arginase, mitochondrial; DE EC=3.5.3.1 {ECO:0000305|PubMed:32754173}; DE AltName: Full=Agmatinase ARGAH {ECO:0000305}; DE EC=3.5.3.11 {ECO:0000250|UniProtKB:P46637}; DE AltName: Full=Arginine amidohydrolase {ECO:0000305}; DE Short=MtARGAH {ECO:0000303|PubMed:32754173}; DE Flags: Precursor; GN Name=ARGAH {ECO:0000303|PubMed:32754173}; GN OrderedLocusNames=MTR_4g024960 {ECO:0000312|EMBL:AES87366.2}; GN ORFNames=MtrunA17_Chr4g0011501 {ECO:0000312|EMBL:RHN59278.1}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). 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; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3880; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Jemalong A17; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H., RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M., RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H., RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C., RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Jemalong A17; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume Medicago RT truncatula."; RL BMC Genomics 15:312-312(2014). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Jemalong A17; RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7; RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S., RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M., RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W., RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F., RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F., RA Benhamed M., Crespi M., Gouzy J., Gamas P.; RT "Whole-genome landscape of Medicago truncatula symbiotic genes."; RL Nat. Plants 4:1017-1025(2018). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH ORNITHINE AND RP MANGANESE IONS, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=32754173; DOI=10.3389/fpls.2020.00987; RA Sekula B.; RT "The neighboring subunit is engaged to stabilize the substrate in the RT active site of plant arginases."; RL Front. Plant Sci. 11:987-987(2020). CC -!- FUNCTION: Catalyzes the hydrolysis of L-arginine to urea and L- CC ornithine (Probable). The latter can be utilized in the urea cycle or CC as a precursor for the synthesis of both polyamines and proline CC (Probable). Possesses agmatinase activity. Catalyzes the formation of CC putrescine from agmatine (By similarity). CC {ECO:0000250|UniProtKB:P46637, ECO:0000305, CC ECO:0000305|PubMed:32754173}. 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:0000305|PubMed:32754173}; CC -!- CATALYTIC ACTIVITY: CC Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145, CC ChEBI:CHEBI:326268; EC=3.5.3.11; CC Evidence={ECO:0000250|UniProtKB:P46637}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742, CC ECO:0000269|PubMed:32754173}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00742, ECO:0000269|PubMed:32754173}; CC -!- PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L- CC arginine: step 1/1. {ECO:0000305}. CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via CC agmatine pathway; putrescine from agmatine: step 1/1. {ECO:0000305}. CC -!- SUBUNIT: Forms homohexamers. {ECO:0000269|PubMed:32754173}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}. CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE- CC ProRule:PRU00742}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM001220; AES87366.2; -; Genomic_DNA. DR EMBL; PSQE01000004; RHN59278.1; -; Genomic_DNA. DR RefSeq; XP_003605169.2; XM_003605121.2. DR PDB; 6VSS; X-ray; 1.93 A; A/B/C/D/E/F=1-338. DR PDB; 6VST; X-ray; 2.12 A; A/B/C/D/E/F/G/H/I/J/K/L=1-338. DR PDBsum; 6VSS; -. DR PDBsum; 6VST; -. DR AlphaFoldDB; G7JFU5; -. DR SMR; G7JFU5; -. DR STRING; 3880.AES87366; -. DR EnsemblPlants; AES87366; AES87366; MTR_4g024960. DR GeneID; 11420737; -. DR Gramene; AES87366; AES87366; MTR_4g024960. DR KEGG; mtr:MTR_4g024960; -. DR eggNOG; KOG2964; Eukaryota. DR HOGENOM; CLU_039478_3_0_1; -. DR OrthoDB; 921352at2759; -. DR UniPathway; UPA00158; UER00270. DR UniPathway; UPA00534; UER00287. DR Proteomes; UP000002051; Chromosome 4. DR Proteomes; UP000265566; Chromosome 4. DR ExpressionAtlas; G7JFU5; differential. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central. DR GO; GO:0004053; F:arginase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019547; P:arginine catabolic process to ornithine; IDA:UniProtKB. DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB. 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 InterPro; IPR020855; Ureohydrolase_Mn_BS. DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1. DR Pfam; PF00491; Arginase; 1. DR PIRSF; PIRSF036979; Arginase; 1. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. DR PROSITE; PS01053; ARGINASE_1; 1. DR PROSITE; PS51409; ARGINASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Arginine metabolism; Hydrolase; Manganese; Metal-binding; KW Mitochondrion; Putrescine biosynthesis; Reference proteome; KW Transit peptide. FT TRANSIT 1..15 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 16..338 FT /note="Arginase, mitochondrial" FT /id="PRO_0000451888" FT BINDING 73 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000269|PubMed:32754173" FT BINDING 92..95 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000269|PubMed:32754173" FT BINDING 157 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 181 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 181 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 183 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 185..187 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000269|PubMed:32754173" FT BINDING 185 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 191..193 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P53608" FT BINDING 220 FT /ligand="L-ornithine" FT /ligand_id="ChEBI:CHEBI:46911" FT /evidence="ECO:0000269|PubMed:32754173" FT BINDING 266 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 266 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 268 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742, FT ECO:0000269|PubMed:32754173" FT BINDING 309 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:32754173" FT HELIX 22..54 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 58..66 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 81..90 FT /evidence="ECO:0007829|PDB:6VSS" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 110..115 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 118..122 FT /evidence="ECO:0007829|PDB:6VSS" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 128..143 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 148..156 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 160..171 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 200..206 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 223..232 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 242..249 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 261..266 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:6VSS" FT TURN 272..274 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:6VST" FT HELIX 288..297 FT /evidence="ECO:0007829|PDB:6VSS" FT STRAND 302..308 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:6VSS" FT HELIX 320..336 FT /evidence="ECO:0007829|PDB:6VSS" SQ SEQUENCE 338 AA; 37199 MW; 4A88C96D0EC88B07 CRC64; MSTIARRGFH YMQRLNSANV SPALLEKAQN RVIDAALTFI RERAKFKGEL MRSLGGVAAT SSLLGVPLGH HSSFHEGSAF APPRIREAIW CDSTNSTTEE GKNLRDPRVI TNVGDVPIEE IRDCGVDDKR LANVISESVK LVMDEDPLRP LVLGGDHSIS FPVVRAVSEK LGGAVDILHF DAHPDLYHDF EGNYYSHASP FARIMEGGYA RRLVQVGIRS ITNDVREQVK KYGVETHEMR TLSRDRPILE NLKLGEGVKG VYVSIDVDSL DPSIAPGVSH HEPGGLLFRD ILNILQNLQG DIVGGDVVEY NPQRDTYDGI TALVAAKLVR ELAAKMSK //