SPEB_SALHS
ID SPEB_SALHS Reviewed; 306 AA.
AC B4THG3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=SeHA_C3316;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001120; ACF67727.1; -; Genomic_DNA.
DR RefSeq; WP_000105550.1; NC_011083.1.
DR AlphaFoldDB; B4THG3; -.
DR SMR; B4THG3; -.
DR KEGG; seh:SeHA_C3316; -.
DR HOGENOM; CLU_039478_0_0_6; -.
DR OMA; YELTTIM; -.
DR UniPathway; UPA00534; UER00287.
DR Proteomes; UP000001866; 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_1000145623"
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; 33603 MW; 6C26A30691F2C3D3 CRC64;
MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR
QVSTNLAWEH HRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLSAGKRML
SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPHH
SVQIGIRTEF DKDNGFTVLD ACQVNDRGVD DILAQVKQIV GDMPVYLTFD IDCLDPAFAP
GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ
AAKKGE
