ID SPEB_SHIB3 Reviewed; 306 AA. AC B2U0V8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=Agmatinase {ECO:0000255|HAMAP-Rule:MF_01418}; DE EC=3.5.3.11 {ECO:0000255|HAMAP-Rule:MF_01418}; DE AltName: Full=Agmatine ureohydrolase {ECO:0000255|HAMAP-Rule:MF_01418}; DE Short=AUH {ECO:0000255|HAMAP-Rule:MF_01418}; GN Name=speB {ECO:0000255|HAMAP-Rule:MF_01418}; GN OrderedLocusNames=SbBS512_E3370; OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=344609; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CDC 3083-94 / BS512; RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R., RA Jiang L., Ravel J., Sebastian Y.; RT "Complete sequence of Shigella boydii serotype 18 strain BS512."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of putrescine from agmatine. CC {ECO:0000255|HAMAP-Rule:MF_01418}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01418}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01418}; CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via CC agmatine pathway; putrescine from agmatine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01418}. CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01418}. 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; CP001063; ACD06722.1; -; Genomic_DNA. DR RefSeq; WP_000105586.1; NC_010658.1. DR AlphaFoldDB; B2U0V8; -. DR SMR; B2U0V8; -. DR STRING; 344609.SbBS512_E3370; -. DR KEGG; sbc:SbBS512_E3370; -. DR HOGENOM; CLU_039478_0_0_6; -. DR UniPathway; UPA00534; UER00287. DR Proteomes; UP000001030; Chromosome. DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IEA:UniProtKB-UniPathway. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd11592; Agmatinase_PAH; 1. DR Gene3D; 3.40.800.10; Ureohydrolase domain; 1. DR HAMAP; MF_01418; SpeB; 1. DR InterPro; IPR023694; Agmatinase. 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 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 3: Inferred from homology; KW Hydrolase; Manganese; Metal-binding; Polyamine biosynthesis; KW Putrescine biosynthesis; Reference proteome; Spermidine biosynthesis. FT CHAIN 1..306 FT /note="Agmatinase" FT /id="PRO_1000145627" FT BINDING 126 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01418" FT BINDING 149 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01418" FT BINDING 151 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01418" FT BINDING 153 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01418" FT BINDING 230 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01418" FT BINDING 232 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01418" SQ SEQUENCE 306 AA; 33534 MW; 4F10509DE8F4CB08 CRC64; MSTLGNQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLAAGKRML SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPNH SVQIGIRTEF DKDNGFTVLD ACQVNDRSVD DVIAQVKQIV GDMPVYLTFD IDCLDPAFAP GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ AAKKGE //