ID Q9RZ04_DEIRA Unreviewed; 304 AA. AC Q9RZ04; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 14-OCT-2008, entry version 48. DE SubName: Full=Agmatinase, putative; GN OrderedLocusNames=DR_A0149; OS Deinococcus radiodurans. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=1299; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1; RX MEDLINE=20036896; 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.A., Utterback T.R., 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.L., 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] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). 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 -!- COFACTOR: Manganese (By similarity). CC -!- SIMILARITY: Belongs to the arginase family. 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; -. 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 GeneID; 1798006; -. DR GenomeReviews; AE001825_GR; DR_A0149. DR KEGG; dra:DR_A0149; -. DR NMPDR; fig|243230.1.peg.2963; -. DR TIGR; DR_A0149; -. DR HOGENOM; Q9RZ04; -. DR BioCyc; DRAD243230:DR_A0149-MON; -. DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrog...; IEA:InterPro. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR InterPro; IPR006035; Ureohydrolase. DR Gene3D; G3DSA:3.40.800.10; Ureohydrolase; 1. DR PANTHER; PTHR11358; Ureohydrolase; 1. DR Pfam; PF00491; Arginase; 1. DR PROSITE; PS00147; ARGINASE_1; 1. DR PROSITE; PS00148; ARGINASE_2; UNKNOWN_1. DR PROSITE; PS01053; ARGINASE_3; UNKNOWN_1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Manganese; Metal-binding. 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 //