ID   SPEB_ECOLC              Reviewed;         306 AA.
AC   B1IT67;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
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}; OrderedLocusNames=EcolC_0774;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-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;
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; CP000946; ACA76446.1; -; Genomic_DNA.
DR   RefSeq; WP_000105566.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IT67; -.
DR   SMR; B1IT67; -.
DR   GeneID; 67415171; -.
DR   KEGG; ecl:EcolC_0774; -.
DR   HOGENOM; CLU_039478_0_0_6; -.
DR   OMA; YELTTIM; -.
DR   UniPathway; UPA00534; UER00287.
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_1000087410"
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