ID   AGUA_LEGPA              Reviewed;         346 AA.
AC   Q5X986;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Putative agmatine deiminase {ECO:0000255|HAMAP-Rule:MF_01841};
DE            EC=3.5.3.12 {ECO:0000255|HAMAP-Rule:MF_01841};
DE   AltName: Full=Agmatine iminohydrolase {ECO:0000255|HAMAP-Rule:MF_01841};
GN   Name=aguA {ECO:0000255|HAMAP-Rule:MF_01841}; OrderedLocusNames=lpp0005;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=agmatine + H2O = N-carbamoylputrescine + NH4(+);
CC         Xref=Rhea:RHEA:18037, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58145, ChEBI:CHEBI:58318; EC=3.5.3.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01841};
CC   -!- SIMILARITY: Belongs to the agmatine deiminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01841}.
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DR   EMBL; CR628336; CAH11153.1; -; Genomic_DNA.
DR   RefSeq; WP_011212651.1; NC_006368.1.
DR   AlphaFoldDB; Q5X986; -.
DR   SMR; Q5X986; -.
DR   KEGG; lpp:lpp0005; -.
DR   LegioList; lpp0005; -.
DR   HOGENOM; CLU_037682_0_0_6; -.
DR   OMA; GNVACIT; -.
DR   GO; GO:0047632; F:agmatine deiminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004668; F:protein-arginine deiminase activity; IEA:InterPro.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01841; Agmatine_deimin; 1.
DR   InterPro; IPR017754; Agmatine_deiminase.
DR   InterPro; IPR007466; Peptidyl-Arg-deiminase_porph.
DR   PANTHER; PTHR31377; PTHR31377; 1.
DR   Pfam; PF04371; PAD_porph; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..346
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194328"
FT   ACT_SITE        333
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   346 AA;  39115 MW;  4D11C74BAFAC8CEC CRC64;
     MNTAPKQYGF YMPAEWYPHE RCWMAWPCHH ETWSKIGLDK AKMAYARVAK AIAQFEPVTL
     LVNPGDEDSA TNLCKGHNIE IISLPINDSW TRDTGATFLI NNEKQLAGVD WIHNAWGGNY
     ADCSLDNLIA SHLIKCTEAQ YFHAPLVMEG GSFHVDGEGT ILTSKECLLN SNRNPHLSQQ
     EIEQYLINYL GAERIIWLNM GLIGDETDGH IDEIATFIAP GKVLCLITKD KEDPNYHRLQ
     ENFEILKSSK DARGRTFEVY TVEQPPATYL NGERLTLSYI NFYMANQGIV MPAFGYESFD
     RLAYQLFVQI FPGYQITQID ALDVFSGGGG IHCITQQQPK SYKLGE