ID   AGUA_VIBPA              Reviewed;         360 AA.
AC   Q87NU5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=VP1773;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000031; BAC60036.1; -; Genomic_DNA.
DR   RefSeq; NP_798152.1; NC_004603.1.
DR   RefSeq; WP_005464515.1; NC_004603.1.
DR   AlphaFoldDB; Q87NU5; -.
DR   SMR; Q87NU5; -.
DR   STRING; 223926.28806765; -.
DR   EnsemblBacteria; BAC60036; BAC60036; BAC60036.
DR   GeneID; 1189280; -.
DR   KEGG; vpa:VP1773; -.
DR   PATRIC; fig|223926.6.peg.1691; -.
DR   eggNOG; COG2957; Bacteria.
DR   HOGENOM; CLU_037682_1_0_6; -.
DR   OMA; WCRDHGP; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..360
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194347"
FT   ACT_SITE        353
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   360 AA;  40172 MW;  635478931FDA1ACB CRC64;
     MKLSTTPAQD GFYFPAEFQP VSEVWLAWPE RKDNWRDDAL PAQETFARIA NLIAEVTKVC
     VAVCSHNFDR ARQMLHSDVR LVEIPFNDAW MRDIGPTVLV NQAGERRGIS WQFNAWGGEY
     NGLYDNWQQD DLVAGSVCDI IGIDYYRAPF VLEGGAIHTD GEGTLYTTEE CLLSPGRNPQ
     LSKAQIEEQL KVYLGIEKII WLPNGLFNDE TDGHVDNLMH VIAPGKVVLS WTDDPSDPQY
     ALSRQAEQVL KSQHDAKGRE IEIVRLPLPG PLHYSEREAN GIDASSGMSR QAGERLSASY
     ANFLIVNGHV FLPMLDEDTD AIAIDILQNA MPEYQIIAIP SREVLLGGGN IHCITQQIPA