ID   SPEB_SERP5              Reviewed;         306 AA.
AC   A8GIX7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   02-SEP-2026, entry version 99.
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=Spro_3972;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(2009).
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}.
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DR   EMBL; CP000826; ABV43067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GIX7; -.
DR   SMR; A8GIX7; -.
DR   STRING; 399741.Spro_3972; -.
DR   PaxDb; 399741-Spro_3972; -.
DR   KEGG; spe:Spro_3972; -.
DR   eggNOG; COG0010; Bacteria.
DR   HOGENOM; CLU_039478_0_0_6; -.
DR   OrthoDB; 9789727at2; -.
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: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; Spermidine biosynthesis.
FT   CHAIN           1..306
FT                   /note="Agmatinase"
FT                   /id="PRO_1000068497"
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;  33374 MW;  C3E196DB927F79E9 CRC64;
     MSTLGHKSDN SLVSNAFGFL RFPLNFMPYD SDAEWVITGI PFDMATSGRA GGRHGPAAIR
     QVSTNLAWEG NRWPWNFDLR DRVNVVDCGD IVFNFGDAQS MSDNLQAHAE KLLAAGKRML
     SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGSQ YDHGTMFFHA PNEGLIDPTH
     SVQIGIRTEY DHDNGFTVLD AAQVNDRSAD DLLAQIKQIV GDMPVYLTFD IDCLDPAFAP
     GTGTPVIGGL TSDRALKLVR GMQSLNIVGM DVVEVAPAYD QSEITALAAA TLGLEMLYLQ
     AAKKTK
//