ID   AGUA_SHEB2              Reviewed;         370 AA.
AC   B8E8S8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=Sbal223_1234;
OS   Shewanella baltica (strain OS223).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=407976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS223;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Brettar I., Rodrigues J., Konstantinidis K.,
RA   Tiedje J.;
RT   "Complete sequence of chromosome of Shewanella baltica OS223.";
RL   Submitted (DEC-2008) 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; CP001252; ACK45744.1; -; Genomic_DNA.
DR   RefSeq; WP_012587100.1; NC_011663.1.
DR   AlphaFoldDB; B8E8S8; -.
DR   SMR; B8E8S8; -.
DR   PRIDE; B8E8S8; -.
DR   EnsemblBacteria; ACK45744; ACK45744; Sbal223_1234.
DR   KEGG; sbp:Sbal223_1234; -.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   Proteomes; UP000002507; 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_1000188415"
FT   ACT_SITE        361
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   370 AA;  40845 MW;  DDB4FD43B08A3E9B CRC64;
     MTNANVDATP LTTKPSQDGF YMPAEWAAQQ AVWMIWPYRP DNWRSAGAYA QATFAKVADA
     IGAATPVYMG VPKAFLAEAK TVMPSHVTLV EMDSNDCWAR DTGPTVVVND NGECRGVDWG
     FNAWGGHNGG LYFPWDKDEQ VAQQMLKQHG FARYSAPLIL EGGSIHVDGE GTCMTSAECL
     LNANRNPDLT KEQIEDLLRD YLNVKQFIWL QDGVYMDETD GHIDNMCCFA RPGEVILHWT
     DDETDPQYSR SKAAFDVLQN TVDAQGRKLK IHLLPQPGPL YCTEEESKGV TEGTGVPRTA
     GERLAGSYVN FLITNNRIVF PLLDPATDDI AAQKLQEIFP EYEIVGVPAR EILLGGGNIH
     CITQQIPSGK