ID A9GD98_SORC5 Unreviewed; 322 AA. AC A9GD98; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 94. DE SubName: Full=Agmatinase {ECO:0000313|EMBL:CAN99327.1}; DE EC=3.5.3.11 {ECO:0000313|EMBL:CAN99327.1}; GN Name=speB2 {ECO:0000313|EMBL:CAN99327.1}; GN OrderedLocusNames=sce9154 {ECO:0000313|EMBL:CAN99327.1}; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So OS ce56)). OC Bacteria; Pseudomonadati; Myxococcota; Polyangia; Polyangiales; OC Polyangiaceae; Sorangium. OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN99327.1, ECO:0000313|Proteomes:UP000002139}; RN [1] {ECO:0000313|EMBL:CAN99327.1, ECO:0000313|Proteomes:UP000002139} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139}; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A., RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., RA Puehler A., Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR036979-1}; CC Note=Binds 2 manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR036979-1}; CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily. CC {ECO:0000256|ARBA:ARBA00009227}. 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; AM746676; CAN99327.1; -; Genomic_DNA. DR RefSeq; WP_012241763.1; NC_010162.1. DR AlphaFoldDB; A9GD98; -. DR STRING; 448385.sce9154; -. DR KEGG; scl:sce9154; -. DR eggNOG; COG0010; Bacteria. DR HOGENOM; CLU_039478_0_0_7; -. DR OrthoDB; 9789727at2; -. DR BioCyc; SCEL448385:SCE_RS46855-MONOMER; -. DR Proteomes; UP000002139; Chromosome. DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR CDD; cd11592; Agmatinase_PAH; 1. DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1. DR InterPro; IPR005925; Agmatinase-rel. DR InterPro; IPR006035; Ureohydrolase. DR InterPro; IPR023696; Ureohydrolase_dom_sf. DR InterPro; IPR020855; Ureohydrolase_Mn_BS. DR NCBIfam; TIGR01230; agmatinase; 1. DR NCBIfam; NF002564; PRK02190.1; 1. DR PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1. DR PANTHER; PTHR11358:SF26; GUANIDINO ACID HYDROLASE, MITOCHONDRIAL; 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 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684}; KW Manganese {ECO:0000256|PIRSR:PIRSR036979-1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR036979-1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002139}. FT BINDING 131 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1" FT BINDING 154 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1" FT BINDING 156 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1" FT BINDING 158 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1" FT BINDING 238 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1" FT BINDING 240 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1" SQ SEQUENCE 322 AA; 34743 MW; 7C0C3A0E68011D92 CRC64; MIVDNAFTAD SLYGVRREPT YSGALSFLRR KYTRDLTGVD VAVTGIPLDT ATSNRPGTRF GPRAVREASA QLAWNRPYGY EFDPLDRLAV VDYGDCVWDY GRPEESPVAI EEHIGRILDA GVTPLSIGGD HFVSYPILRA VSKRRGKLSL IHFDAHSDTW SDEVGSGRVD HGTMFFHAAR EGLVEPSRSA QIGLRTYNAD TLGFQVLDAP WVHRHGARAV IEHVRNIVGD HEVYLTFDID FLDPSFAPGT GTPVCGGMST AVALEILRGL QGIALVGMDV VEVAPAYDVG EITALAGATI AQEGLGLIAC RPGAPKAREP AG //