ID   AGUA_SHEON              Reviewed;         370 AA.
AC   Q8EIF2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 98.
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=SO_0887;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN53963.2; -; Genomic_DNA.
DR   RefSeq; NP_716518.2; NC_004347.2.
DR   RefSeq; WP_011071176.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EIF2; -.
DR   SMR; Q8EIF2; -.
DR   STRING; 211586.SO_0887; -.
DR   PaxDb; Q8EIF2; -.
DR   KEGG; son:SO_0887; -.
DR   PATRIC; fig|211586.12.peg.852; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; GNVACIT; -.
DR   OrthoDB; 771174at2; -.
DR   PhylomeDB; Q8EIF2; -.
DR   BioCyc; SONE211586:G1GMP-829-MON; -.
DR   Proteomes; UP000008186; 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_0000194341"
FT   ACT_SITE        361
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   370 AA;  40794 MW;  CCDB60F8E2FE34A9 CRC64;
     MTNVNVDVTP LTTKPSQDGF YMPAEWAAQQ AVWMIWPYRP DNWRAAGAYA QATFAKVVDA
     IGAATPVYMG VPKAFLAKAK TVMPSHVTLV EMDSNDCWAR DTGPTVVVNA EGECRGVDWG
     FNAWGGHNGG LYFPWDKDEQ VAQQMLAQHG FARYRAPLIL EGGSIHVDGE GTCMTSAECL
     LNANRNPELT KEQIEGLLRD YLNVKQFIWL QDGVYMDETD GHIDNMCCFA RPGEVILHWT
     DDESDPQYPR SKAALEVLQN TVDAQGRKLK IHLLPQPGPL YCSEEESKGV TEGTGVPRTA
     GERLAGSYVN FLITNHRIVF PLLDPATDDI AAQKLQEIFP EHEIVGVPAR EILLGGGNIH
     CITQQIPAGK