ID   SPEB_SALG2              Reviewed;         306 AA.
AC   B5RE39;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=SG2973;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933173; CAR38778.1; -; Genomic_DNA.
DR   RefSeq; WP_000105553.1; NC_011274.1.
DR   AlphaFoldDB; B5RE39; -.
DR   SMR; B5RE39; -.
DR   KEGG; seg:SG2973; -.
DR   HOGENOM; CLU_039478_0_0_6; -.
DR   UniPathway; UPA00534; UER00287.
DR   Proteomes; UP000008321; 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_1000145622"
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;  33576 MW;  23E6500AA131CB8F CRC64;
     MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR
     QVSTNLAWEH HRFPWSFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLSAGKRML
     SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPHH
     SVQIGIRTEF DKDNGFTVLD ACQVNDRGVD DILAQVKQIV GDMPVYLTFD IDCLDPAFAP
     GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ
     AAKKGE
//