ID   AGUA_SHEFN              Reviewed;         370 AA.
AC   Q083U9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Sfri_1615;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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; CP000447; ABI71466.1; -; Genomic_DNA.
DR   RefSeq; WP_011637082.1; NC_008345.1.
DR   AlphaFoldDB; Q083U9; -.
DR   SMR; Q083U9; -.
DR   STRING; 318167.Sfri_1615; -.
DR   EnsemblBacteria; ABI71466; ABI71466; Sfri_1615.
DR   KEGG; sfr:Sfri_1615; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; GNVACIT; -.
DR   OrthoDB; 771174at2; -.
DR   Proteomes; UP000000684; 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..370
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_1000070569"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        361
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   370 AA;  40609 MW;  8FF106870DC2DA92 CRC64;
     MTNMNVDATQ LTTKPSQDGF SMPAEWAQQQ AVWMIWPYRP DNWRSAGAYA QATFAKVADA
     IGAVTPVYMG VPKAFLAQAK TVMPAHVTLV EIDSNDCWAR DTGPTVVVNA KGECRGVDWG
     FNAWGGDNGG LYSPWDKDEL VAQKMLTQHG FDRYQAPLIL EGGSIHVDGE GTCMTTAECL
     LNSNRNPDLT REQIEALLAE YLNVKQFIWL PDGVYMDETD GHIDNLCCFA RPGEVVLHWT
     DDQSDPQYPR SKAALDILQN TVDAQGRKLT VHLIPQPGPL YCTEEEAQGV AEGTGVPRTA
     GERLAGSYAN FLITNNRIVF PLLDPVTDDI AAQKLQEIFP EYEIVGVPAR EILLGGGNIH
     CITQQIPSGK