ID SPEB_ENT38 Reviewed; 306 AA. AC A4WE75; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 104. 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=Ent638_3343; OS Enterobacter sp. (strain 638). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=638; RX PubMed=20485560; DOI=10.1371/journal.pgen.1000943; RA Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D., RA Vangronsveld J., Newman L., Monchy S.; RT "Genome sequence of the plant growth promoting endophytic bacterium RT Enterobacter sp. 638."; RL PLoS Genet. 6:E1000943-E1000943(2010). 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; CP000653; ABP62005.1; -; Genomic_DNA. DR RefSeq; WP_015960333.1; NC_009436.1. DR AlphaFoldDB; A4WE75; -. DR SMR; A4WE75; -. DR STRING; 399742.Ent638_3343; -. DR GeneID; 66409687; -. DR KEGG; ent:Ent638_3343; -. DR eggNOG; COG0010; Bacteria. DR HOGENOM; CLU_039478_0_0_6; -. DR OrthoDB; 9789727at2; -. DR UniPathway; UPA00534; UER00287. DR Proteomes; UP000000230; 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; Spermidine biosynthesis. FT CHAIN 1..306 FT /note="Agmatinase" FT /id="PRO_1000068496" 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; 33481 MW; 5B8DFD35A898C936 CRC64; MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLAAGKRML SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PNEGLIDPNH SVQIGIRTEF DKDNGFTVLD AGQVNDRGVD DIIAQVKQIV GDMPVYLTFD IDCLDPAFAP GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ AAKKGE //