ID SPEB_ECO57 Reviewed; 306 AA. AC P60652; P16936; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2004, sequence version 1. DT 02-SEP-2026, entry version 129. 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=Z4281, ECs3812; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: Catalyzes the formation of putrescine from agmatine. CC {ECO:0000255|HAMAP-Rule:MF_01418}. CC -!- CATALYTIC ACTIVITY: CC Reaction=agmatine + H2O = urea + putrescine; 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; AE005174; AAG58067.1; -; Genomic_DNA. DR EMBL; BA000007; BAB37235.1; -; Genomic_DNA. DR PIR; D91105; D91105. DR RefSeq; NP_311839.1; NC_002695.2. DR RefSeq; WP_000105566.1; NZ_AP018488.1. DR AlphaFoldDB; P60652; -. DR SMR; P60652; -. DR STRING; 155864.Z4281; -. DR GeneID; 67175587; -. DR GeneID; 89517749; -. DR GeneID; 916365; -. DR KEGG; ece:Z4281; -. DR KEGG; ecs:ECs_3812; -. DR PATRIC; fig|386585.9.peg.3979; -. DR eggNOG; COG0010; Bacteria. DR HOGENOM; CLU_039478_0_0_6; -. DR OMA; YELTTIM; -. DR UniPathway; UPA00534; UER00287. DR Proteomes; UP000000558; Chromosome. DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro. DR GO; GO:0009446; P:putrescine biosynthetic process; IEA:InterPro. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd11592; Agmatinase_PAH; 1. DR FunFam; 3.40.800.10:FF:000001; Agmatinase; 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 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; Manganese; Metal-binding; Polyamine biosynthesis; KW Putrescine biosynthesis; Reference proteome; Spermidine biosynthesis. FT CHAIN 1..306 FT /note="Agmatinase" FT /id="PRO_0000173732" 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; 33557 MW; 48208BF2CF155570 CRC64; MSTLGHQYDN 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 //