ID Q9RZ04_DEIRA Unreviewed; 304 AA. AC Q9RZ04; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 146. DE SubName: Full=Agmatinase, putative {ECO:0000313|EMBL:AAF12214.1}; GN OrderedLocusNames=DR_A0149 {ECO:0000313|EMBL:AAF12214.1}; OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF12214.1, ECO:0000313|Proteomes:UP000002524}; RN [1] {ECO:0000313|EMBL:AAF12214.1, ECO:0000313|Proteomes:UP000002524} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524}; RX PubMed=10567266; DOI=10.1126/science.286.5444.1571; RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C., RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C., RA Fraser C.M.; RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans RT R1."; RL Science 286:1571-1577(1999). RN [2] {ECO:0007829|PDB:1WOG, ECO:0007829|PDB:1WOH} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MANGANESE. RX PubMed=15355972; DOI=10.1074/jbc.M409246200; RA Ahn H.J., Kim K.H., Lee J., Ha J.Y., Lee H.H., Kim D., Yoon H.J., RA Kwon A.R., Suh S.W.; RT "Crystal structure of agmatinase reveals structural conservation and RT inhibition mechanism of the ureohydrolase superfamily."; RL J. Biol. Chem. 279:50505-50513(2004). CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE- CC ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}. 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; AE001825; AAF12214.1; -; Genomic_DNA. DR PIR; H75610; H75610. DR RefSeq; NP_285473.1; NC_001264.1. DR RefSeq; WP_010889409.1; NZ_JMLF01000008.1. DR PDB; 1WOG; X-ray; 1.80 A; A/B/C/D/E/F=1-304. DR PDB; 1WOH; X-ray; 1.75 A; A/B/C/D/E/F=1-304. DR PDB; 1WOI; X-ray; 1.85 A; A/B/C/D/E/F=1-304. DR PDBsum; 1WOG; -. DR PDBsum; 1WOH; -. DR PDBsum; 1WOI; -. DR AlphaFoldDB; Q9RZ04; -. DR SMR; Q9RZ04; -. DR STRING; 243230.DR_A0149; -. DR DrugBank; DB03260; Hexamethylene diamine. DR PaxDb; 243230-DR_A0149; -. DR EnsemblBacteria; AAF12214; AAF12214; DR_A0149. DR GeneID; 69519044; -. DR KEGG; dra:DR_A0149; -. DR PATRIC; fig|243230.17.peg.3036; -. DR eggNOG; COG0010; Bacteria. DR HOGENOM; CLU_039478_0_2_0; -. DR InParanoid; Q9RZ04; -. DR OMA; CIDAGFV; -. DR OrthoDB; 9788689at2; -. DR EvolutionaryTrace; Q9RZ04; -. DR Proteomes; UP000002524; Chromosome II. DR GO; GO:0008783; F:agmatinase activity; IBA:GO_Central. 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 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:SF26; AGMATINASE, MITOCHONDRIAL; 1. 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 {ECO:0007829|PDB:1WOG, ECO:0007829|PDB:1WOH}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:1WOG}; KW Reference proteome {ECO:0000313|Proteomes:UP000002524}. FT BINDING 121 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1WOG, ECO:0007829|PDB:1WOI" FT BINDING 143 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1WOI" FT BINDING 143 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1WOG, ECO:0007829|PDB:1WOI" FT BINDING 145 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1WOI" FT BINDING 147 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1WOG, ECO:0007829|PDB:1WOI" FT BINDING 229 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1WOI" FT BINDING 229 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1WOG, ECO:0007829|PDB:1WOI" FT BINDING 231 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1WOI" SQ SEQUENCE 304 AA; 32523 MW; 97F826881D581182 CRC64; MSGPAHLPYG GIPTFARAPL VQPDGDWQAD VAALGVPFDI ALGFRPGARF APRALREASL RSVPPFTGLD GKTRLQGVTF ADAGDVILPS LEPQLAHDRI TEAARQVRGR CRVPVFLGGD HSVSYPLLRA FADVPDLHVV QLDAHLDFTD TRNDTKWSNS SPFRRACEAL PNLVHITTVG LRGLRFDPEA VAAARARGHT IIPMDDVTAD LAGVLAQLPR GQNVYFSVDV DGFDPAVIPG TSSPEPDGLT YAQGMKILAA AAANNTVVGL DLVELAPNLD PTGRSELLMA RLVMETLCEV FDHV //