SPEB_ECO27
ID SPEB_ECO27 Reviewed; 306 AA.
AC B7UHY3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=E2348C_3189;
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(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; FM180568; CAS10737.1; -; Genomic_DNA.
DR RefSeq; WP_000105562.1; NC_011601.1.
DR AlphaFoldDB; B7UHY3; -.
DR SMR; B7UHY3; -.
DR EnsemblBacteria; CAS10737; CAS10737; E2348C_3189.
DR KEGG; ecg:E2348C_3189; -.
DR HOGENOM; CLU_039478_0_0_6; -.
DR OMA; YELTTIM; -.
DR UniPathway; UPA00534; UER00287.
DR Proteomes; UP000008205; 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_1000184846"
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; 33571 MW; 5B98B07164854B9F CRC64;
MSTLGHQYDN SLVSNAFGFL RLPMNFQPYD SDADWVITGV PFDMATSGRA GGRHGPAAIR
QVSTNLAWEH NRFPWNFDMR ERLNVVDCGD LVYAFGDARE MSEKLQAHAE KLLAAGKRML
SFGGDHFVTL PLLRAHAKHF GKMALVHFDA HTDTYANGCE FDHGTMFYTA PKEGLIDPNH
SVQIGIRTEF DKDNGFTVLD ACQVNDRSVD DIIAQVKQIV GDMPVYLTFD IDCLDPAFAP
GTGTPVIGGL TSDRAIKLVR GLKDLNIVGM DVVEVAPAYD QSEITALAAA TLALEMLYIQ
AAKKGE