ID   SPEB_PROMI              Reviewed;         306 AA.
AC   Q7X3P1;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Agmatinase;
DE            EC=3.5.3.11;
DE   AltName: Full=Agmatine ureohydrolase;
DE            Short=AUH;
GN   Name=speB;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RX   PubMed=14756784; DOI=10.1046/j.1365-2958.2003.03835.x;
RA   Sturgill G., Rather P.N.;
RT   "Evidence that putrescine acts as an extracellular signal required for
RT   swarming in Proteus mirabilis.";
RL   Mol. Microbiol. 51:437-446(2004).
CC   -!- FUNCTION: Catalyzes the formation of putrescine from agmatine.
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       agmatine pathway; putrescine from agmatine: step 1/1.
CC   -!- DISRUPTION PHENOTYPE: Cells show a delay in differentiation to swarmer
CC       cells and are unable to migrate effectively on agar surfaces.
CC       Putrescine restores normal cell differentiation and migration ability.
CC       {ECO:0000269|PubMed:14756784}.
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP55488.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY298901; AAP55488.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004248574.1; NZ_WURR01000002.1.
DR   AlphaFoldDB; Q7X3P1; -.
DR   SMR; Q7X3P1; -.
DR   STRING; 584.AOUC001_04320; -.
DR   GeneID; 6803298; -.
DR   PATRIC; fig|584.106.peg.2571; -.
DR   OMA; YELTTIM; -.
DR   OrthoDB; 1598732at2; -.
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_0000173738"
FT   BINDING         128
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   306 AA;  33473 MW;  BFAD491A8881C77B CRC64;
     MKNCTLGNET DNSLISNAFG FLRFPLNFQP YSSDADWVIT GVPFDMATSG RAGTRHGPGA
     IRQISTNLAW EGHRWPWHFD MRERLKVVDC GDLVFNFGDA QDMSDKLQAH TEKLLAAGKR
     CLTFGGDHFV TLPLLRAHAK HFGKMALVHF DAHTDTYANG SKFDHGTMFY HAPNEGLIDP
     QHSVQIGIRT EHDTNNGFTV LDAAQVNDRG VDDLVAQIKE IVGSLPVYLT FDIDCLDPAF
     APGTGTPVVG GLTTDKALKM LRALQPLNIV GMDLVEVSPA YDQSDITALA GATIALDMLY
     LQAAKK