(data stored in ACNUC10821 zone)

SWISSPROT: AGUA2_LISMF

ID   AGUA2_LISMF             Reviewed;         369 AA.
AC   Q725C4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 74.
DE   RecName: Full=Putative agmatine deiminase 2 {ECO:0000255|HAMAP-Rule:MF_01841};
DE            EC=3.5.3.12 {ECO:0000255|HAMAP-Rule:MF_01841};
DE   AltName: Full=Agmatine iminohydrolase 2 {ECO:0000255|HAMAP-Rule:MF_01841};
GN   Name=aguA2 {ECO:0000255|HAMAP-Rule:MF_01841};
GN   OrderedLocusNames=LMOf2365_0049;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(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}.
DR   EMBL; AE017262; AAT02837.1; -; Genomic_DNA.
DR   RefSeq; WP_003727552.1; NC_002973.6.
DR   SMR; Q725C4; -.
DR   EnsemblBacteria; AAT02837; AAT02837; LMOf2365_0049.
DR   KEGG; lmf:LMOf2365_0049; -.
DR   HOGENOM; HOG000239346; -.
DR   KO; K10536; -.
DR   OMA; FCASYTN; -.
DR   BioCyc; LMON265669:G1G0V-49-MONOMER; -.
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;
DR   PRODOM; Q725C4.
DR   SWISS-2DPAGE; Q725C4.
KW   Hydrolase.
FT   CHAIN           1..369
FT                   /note="Putative agmatine deiminase 2"
FT                   /id="PRO_0000194332"
FT   ACT_SITE        356
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   369 AA;  42089 MW;  3200DA2DE77ABAF4 CRC64;
     MGQLKGLPVE DGFRMPGEYE PHIGCFMIWP ERPDNWRLGG KPAQQNYKEV AVAISNFEPV
     TMFVSPNQYK NARKELPDTI RVIEMSNDDA WIRDYGPSFL VNDKGEMRGV DWGFNAWGGL
     LDGLYFPWDK DNQIAKKVCD LERLDYYSQK DFILEGCSIH VDGEGTLVTT EECLLSEGRN
     PNLTKIEIEQ TLKKYFHVQK VIWLKHGFYL DETNGHVDNI FNFVAPGEVV LSWTDNKSDP
     QYEISRECYD ILANQTDAKG RTFMIHKLHC PDPVLITQTE SEGVEAINGT FPRQAGDRLA
     ASYVNYYTAN GAIIFPLFDD PKDKDAQELL EQLYPDRKIV GIKAREILLG GGNIHCITQH
     LPDKSTIRE
//

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