ID   AGUA_LEGPH              Reviewed;         348 AA.
AC   Q5ZZK4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=lpg0005;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(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; AE017354; AAU26113.1; -; Genomic_DNA.
DR   RefSeq; YP_094060.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZZK4; -.
DR   SMR; Q5ZZK4; -.
DR   STRING; 272624.lpg0005; -.
DR   PaxDb; Q5ZZK4; -.
DR   PRIDE; Q5ZZK4; -.
DR   EnsemblBacteria; AAU26113; AAU26113; lpg0005.
DR   KEGG; lpn:lpg0005; -.
DR   PATRIC; fig|272624.6.peg.5; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_0_0_6; -.
DR   OMA; WCRDHGP; -.
DR   Proteomes; UP000000609; 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; Reference proteome.
FT   CHAIN           1..348
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194329"
FT   ACT_SITE        335
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   348 AA;  39479 MW;  987298737D9E5C28 CRC64;
     MNMNTAPKQY GFYMPAEWYP HERCWMAWPC HHETWSKIGL DKAKMAYARV AKAIAQFEPV
     TLLVNPGDED SAENLCKGHN IEIISLPIND SWTRDTGATF LINNERQLAG VDWIHNAWGG
     NYADCSLDNL IASHLIKYTE AQYFHAPLVM EGGSFHVDGE GTILTSKECL LNSNRNPHLS
     QQEIEQYLIN YLGAERIIWL NMGLIGDETD GHVDEIATFI APGKVLCLIT KDKEDPNYHR
     LQENFEILKS SKDARGRTFE VYTVEQPPAT YLNGERLTLS YINFYMANQG IVMPAFGYES
     FDRLAYQLFV QIFPGYQITQ IDALDVFSGG GGIHCITQQQ PKSHKLVE