ID Q9RZ04_DEIRA Unreviewed; 304 AA. AC Q9RZ04; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 30-NOV-2016, entry version 114. 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 / OS LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422). OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; 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 RT radiodurans R1."; RL Science 286:1571-1577(1999). RN [2] {ECO:0000213|PDB:1WOG, ECO:0000213|PDB:1WOH, ECO:0000213|PDB:1WOI} 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. CC {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_CP015082.1. 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 ProteinModelPortal; Q9RZ04; -. DR SMR; Q9RZ04; -. DR STRING; 243230.DR_A0149; -. DR EnsemblBacteria; AAF12214; AAF12214; DR_A0149. DR GeneID; 1798006; -. DR KEGG; dra:DR_A0149; -. DR PATRIC; 21633334; VBIDeiRad64572_3036. DR eggNOG; ENOG4105CYW; Bacteria. DR eggNOG; COG0010; LUCA. DR HOGENOM; HOG000204320; -. DR InParanoid; Q9RZ04; -. DR KO; K01480; -. DR OMA; EHWDFDL; -. DR OrthoDB; POG091H0384; -. DR BioCyc; DRAD243230:GH46-2836-MONOMER; -. DR EvolutionaryTrace; Q9RZ04; -. DR Proteomes; UP000002524; Chromosome II. DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.800.10; -; 1. DR InterPro; IPR006035; Ureohydrolase. DR InterPro; IPR023696; Ureohydrolase_domain. DR InterPro; IPR020855; Ureohydrolase_Mn_BS. DR PANTHER; PTHR11358; PTHR11358; 1. DR Pfam; PF00491; Arginase; 1. DR PIRSF; PIRSF036979; Arginase; 1. DR PROSITE; PS01053; ARGINASE_1; 1. DR PROSITE; PS51409; ARGINASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1WOG, ECO:0000213|PDB:1WOH, KW ECO:0000213|PDB:1WOI}; KW Complete proteome {ECO:0000313|Proteomes:UP000002524}; KW Hydrolase {ECO:0000256|RuleBase:RU003684}; KW Manganese {ECO:0000213|PDB:1WOG, ECO:0000213|PDB:1WOI}; KW Metal-binding {ECO:0000213|PDB:1WOG, ECO:0000213|PDB:1WOI}; KW Reference proteome {ECO:0000313|Proteomes:UP000002524}. FT METAL 121 121 Manganese 1; via pros nitrogen. FT {ECO:0000213|PDB:1WOG, ECO:0000213|PDB: FT 1WOI}. FT METAL 143 143 Manganese 1. {ECO:0000213|PDB:1WOG, FT ECO:0000213|PDB:1WOI}. FT METAL 143 143 Manganese 2. {ECO:0000213|PDB:1WOG, FT ECO:0000213|PDB:1WOI}. FT METAL 145 145 Manganese 2; via pros nitrogen. FT {ECO:0000213|PDB:1WOG, ECO:0000213|PDB: FT 1WOI}. FT METAL 147 147 Manganese 1. {ECO:0000213|PDB:1WOG, FT ECO:0000213|PDB:1WOI}. FT METAL 229 229 Manganese 1. {ECO:0000213|PDB:1WOG, FT ECO:0000213|PDB:1WOI}. FT METAL 229 229 Manganese 2. {ECO:0000213|PDB:1WOG, FT ECO:0000213|PDB:1WOI}. FT METAL 231 231 Manganese 2. {ECO:0000213|PDB:1WOG, FT ECO:0000213|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 //