ID   AGUA2_LISMO             Reviewed;         369 AA.
AC   Q8YAS3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative agmatine deiminase 2 {ECO:0000255|HAMAP-Rule:MF_01841};
DE            EC=3.5.3.12 {ECO:0000255|HAMAP-Rule:MF_01841};
DE   AltName: Full=Agmatine iminohydrolase 2 {ECO:0000255|HAMAP-Rule:MF_01841};
GN   Name=aguA2 {ECO:0000255|HAMAP-Rule:MF_01841}; OrderedLocusNames=lmo0040;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591973; CAC98255.1; -; Genomic_DNA.
DR   PIR; AI1079; AI1079.
DR   RefSeq; NP_463573.1; NC_003210.1.
DR   RefSeq; WP_009911777.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8YAS3; -.
DR   SMR; Q8YAS3; -.
DR   STRING; 169963.lmo0040; -.
DR   PaxDb; Q8YAS3; -.
DR   EnsemblBacteria; CAC98255; CAC98255; CAC98255.
DR   GeneID; 985194; -.
DR   KEGG; lmo:lmo0040; -.
DR   PATRIC; fig|169963.11.peg.41; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_9; -.
DR   OMA; GNVACIT; -.
DR   PhylomeDB; Q8YAS3; -.
DR   BioCyc; LMON169963:LMO0040-MON; -.
DR   Proteomes; UP000000817; 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.
DR   TIGRFAMs; TIGR03380; agmatine_aguA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..369
FT                   /note="Putative agmatine deiminase 2"
FT                   /id="PRO_0000194334"
FT   ACT_SITE        356
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   369 AA;  42044 MW;  E28CDDB2751B1ECB CRC64;
     MGQLKGLPVE DGFRMPGEYE PHIGCFMIWP ERPDNWRLGG KPAQQNYKEV AVAISNFEPV
     TMFVSPNQYK NARKELPDTI RVIEMSNDDA WIRDYGPSFL VDDKGDMRGV DWGFNAWGGL
     LDGLYFPWDK DNQIAKKVCE LERIDYYSQK DFILEGCSIH VDGEGTLVTT EECLLSEGRN
     PNLTKIEIEQ TLKKYFHAQK VIWLKHGFYL DETNGHVDNI FNFVAPGEVV LSWTDNKSDP
     QYEISRECYD ILANKTDAKG RTFIIHKLHC PDPVLITQTE SEGVEAINGT FPRQAGDRLA
     ASYVNYYTAN GAIIFPLFDD PKDKDAQELL EKLYPDRKIV GIKAREILLG GGNIHCITQH
     LPDKSTIRE