ID   AGUA_LEGPL              Reviewed;         347 AA.
AC   Q5X0L4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=lpl0005;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
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}.
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; CR628337; CAH14235.1; -; Genomic_DNA.
DR   RefSeq; WP_011214299.1; NC_006369.1.
DR   AlphaFoldDB; Q5X0L4; -.
DR   SMR; Q5X0L4; -.
DR   EnsemblBacteria; CAH14235; CAH14235; lpl0005.
DR   KEGG; lpf:lpl0005; -.
DR   LegioList; lpl0005; -.
DR   HOGENOM; CLU_037682_0_0_6; -.
DR   OMA; WCRDHGP; -.
DR   Proteomes; UP000002517; Chromosome.
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..347
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194330"
FT   ACT_SITE        333
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   347 AA;  39395 MW;  3D30FA52607CB5BE CRC64;
     MNTAPKQYGF YMPAEWYPHE RCWMAWPCHH ETWSKIGLDK AKMAYARVAK AIAQFEPVTL
     LVNPGDEDSA KNLCKGHNIE IISLPINDSW TRDTGATFLI NNERQLAGVD WIHNAWGGNY
     ADCSLDNFIA SHIIKYTEAQ YFHAPLVMEG GSFHVDGEGT ILTSKECLLN SNRNPHLSQQ
     EIEQYLINYL GAERIIWLNM GLIGDETDGH VDEIATFIAP GKVLCLITKD KEDPNYHRLQ
     ENFEILKSSK DARGRTFEVY TVEQPPATYL NGERLTLSYI NFYMANQGIV MPAFGYESFD
     RLAYQLFVQI FPGYQITQID ALDVFSGGGG IHCITQQQPK SHKLVEQ