ID   AGUA_YERPS              Reviewed;         365 AA.
AC   Q666N7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 76.
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=YPTB3211;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH22449.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX936398; CAH22449.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q666N7; -.
DR   SMR; Q666N7; -.
DR   EnsemblBacteria; CAH22449; CAH22449; YPTB3211.
DR   KEGG; yps:YPTB3211; -.
DR   OMA; WCRDHGP; -.
DR   Proteomes; UP000001011; 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..365
FT                   /note="Putative agmatine deiminase"
FT                   /id="PRO_0000194349"
FT   ACT_SITE        357
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   365 AA;  40377 MW;  8A188EE380CA3798 CRC64;
     MLQQQALPGT PRQDGFFMPA EWAPQDAVWM LWPYRQDNWR GKAIPAQQTF AKVAEAISRA
     TPVFMGVPAE FMAQAKATMP ANVTLVEMAS DDAWMRDTGP TMVINGAAER RAVDWQFNAW
     GGLNGGLYAD WQQDEKVAVQ VSDFLKNAHY SAPLILEGGS IHTDGEGTLL TTAECLLNPN
     RNPHLNQAQI EQLLCDYLGV THFIWLQDGV YNDETDGHID NMCCFVRPGE VALHWTDDQQ
     DPQYARSVAA FEVLSNTVDA KGRKLKIWKL PAPGPLYNTE EETFDVLTSD AVPRTAGERL
     AGSYVNFLIS NQQIIFPLLD SRTDGQANDL LQQMFPGYAI VGVPAREILL GGGNIHCITQ
     QIPAA