ID   AGUA_SELRU              Reviewed;         371 AA.
AC   Q5KR05;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 41.
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};
OS   Selenomonas ruminantium.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Selenomonas.
OX   NCBI_TaxID=971;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Liao S., Takatsuka Y., Yamakuchi Y., Abe N., Kamio Y.;
RT   "Gene cloning and molecular characterization of arginine decarboxylase from
RT   Selenomonas ruminantium.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB198395; BAD86640.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5KR05; -.
DR   SMR; Q5KR05; -.
DR   OMA; WCRDHGP; -.
DR   BRENDA; 3.5.3.12; 5668.
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.
FT   CHAIN           1..371
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194340"
FT   ACT_SITE        361
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   371 AA;  41392 MW;  162C0EED78DDBADC CRC64;
     MMIKDSTPKA DGFYMPAEFS PHAGTFLIWP VRPGSWTNAG ADVQPVFVEL IREISAVEEL
     YLLVDEAHRP QAENMLKDLP QQHIHYLAIP TDDAWARDMG PTYVIDGQGR RRGINWRFNA
     WGGDFDGLYP DYGQDDAAAE KMCAALGDEL YDAGDFVLEG GSIHVDGEGT VVVTEACLLS
     QGRNPDLSKE QIEAMLLKYL GAEKVIWLPR GIHNDETNEH VDNVFAFVRP GEVLLAWTDD
     KDDPQYELSQ ADLEVLESAT DARGRKFVIH KLPIPQEPVC ITAEEADSFT FEEGEDRREP
     GERLAASYVN FYLCNGKVIL PQFGDEMDIE AQRILGKCFP ERKVVPLPAK AVIVGGGNFH
     CLTQQIPAIE R