ID   SPEB_ECO55              Reviewed;         306 AA.
AC   B7LFJ6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=EC55989_3229;
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CU928145; CAU99217.1; -; Genomic_DNA.
DR   RefSeq; WP_000105559.1; NC_011748.1.
DR   AlphaFoldDB; B7LFJ6; -.
DR   SMR; B7LFJ6; -.
DR   EnsemblBacteria; CAU99217; CAU99217; EC55989_3229.
DR   KEGG; eck:EC55989_3229; -.
DR   HOGENOM; CLU_039478_0_0_6; -.
DR   OMA; YELTTIM; -.
DR   UniPathway; UPA00534; UER00287.
DR   Proteomes; UP000000746; 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   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   PANTHER; PTHR11358; PTHR11358; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   SUPFAM; SSF52768; SSF52768; 1.
DR   TIGRFAMs; TIGR01230; agmatinase; 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_1000184847"
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;  33542 MW;  1A208A7CF478E3AB CRC64;
     MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR
     QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLAAGKRML
     SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPNH
     SVQIGIRTEF DIDNGFTVLD ACQVNDRSVD DVIAQVKQIV GDMPVYLTFD IDCLDPAFAP
     GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ
     AAKKGE