ID   AGUA_SHEB9              Reviewed;         370 AA.
AC   A9KYH3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
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};
GN   OrderedLocusNames=Sbal195_3282;
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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; CP000891; ABX50444.1; -; Genomic_DNA.
DR   RefSeq; WP_012197447.1; NC_009997.1.
DR   AlphaFoldDB; A9KYH3; -.
DR   SMR; A9KYH3; -.
DR   EnsemblBacteria; ABX50444; ABX50444; Sbal195_3282.
DR   GeneID; 11773335; -.
DR   KEGG; sbn:Sbal195_3282; -.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   Proteomes; UP000000770; 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.
FT   CHAIN           1..370
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_1000088467"
FT   ACT_SITE        361
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   370 AA;  40824 MW;  4E6538AE072764C7 CRC64;
     MTNANVDATQ LTTKPSQDGF YMPAEWAAQQ AVWMIWPYRP DNWRSAGAYA QATFAKVADA
     IGGATPVYMG VPKAFLAEAK TVMPSHVTLV EMDSNDCWAR DTGPTVVVNA EGECRGVDWG
     FNAWGGHNGG LYFPWDKDEQ VAQQMLKQHG FARYSAPLIL EGGSIHVDGE GTCMTSAECL
     LNANRNPDLT KEQIEDLLRD YLNVKQFIWL QDGVYMDETD GHIDNMCCFA RPGEVILHWT
     DDETDPQYPR SKAALDVLQN TVDAQGRKLK IHLLPQPGPL YCTEEESLGV TEGTGVPRTA
     GERLAGSYVN FLITNNRIVF PLLDPTTDDI AAQKLQEIFP EYEIVGVPAR EILLGGGNIH
     CITQQIPSGK