ID   AGUA_LACLA              Reviewed;         366 AA.
AC   Q9CEY6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=LL1697;
GN   ORFNames=L136332;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(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; AE005176; AAK05795.1; -; Genomic_DNA.
DR   PIR; A86837; A86837.
DR   RefSeq; NP_267853.1; NC_002662.1.
DR   RefSeq; WP_003130391.1; NC_002662.1.
DR   AlphaFoldDB; Q9CEY6; -.
DR   SMR; Q9CEY6; -.
DR   STRING; 272623.L136332; -.
DR   PaxDb; Q9CEY6; -.
DR   EnsemblBacteria; AAK05795; AAK05795; L136332.
DR   KEGG; lla:L136332; -.
DR   PATRIC; fig|272623.7.peg.1821; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_9; -.
DR   OMA; IDFRFCE; -.
DR   Proteomes; UP000002196; 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..366
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194326"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   366 AA;  41268 MW;  FF7A6FD38D4476ED CRC64;
     MAKRIIGTTP KEDGFRMPGE FEAQDQIFMI WPERPDNWRD GAKPVQIAFT NVAKAISRFT
     PVTMLVSQSQ YQNARYQLPA DVRVLEVSNN DSWVRDCGPS FVINDKGELR ANDWTFNAWG
     GLVDGLYFPW DQDDLVAQKV CELERVDSYR TDDFVLEGGS FHVDGQGTVL TTEMCLLSEG
     RNPHMSKEDI ENKLKEHLNA EKILWLGDGI DPEETNGHVD DVACFVAPGE VACIYTEDEK
     SPFYEAAQDA YKRLNQMTDA KGRQLKVHKL TCPAKNVTIK KQFRIDTVEG TMPREDGDIC
     IASYMNFLIT NKGVIVPQYG DENDALALKQ VQEMFPDREI VGVNTVEVVY GGGNIHCITQ
     QQPKAK