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 25-MAY-2022, entry version 81.
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}.
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DR EMBL; AE017262; AAT02837.1; -; Genomic_DNA.
DR RefSeq; WP_003727552.1; NC_002973.6.
DR AlphaFoldDB; Q725C4; -.
DR SMR; Q725C4; -.
DR PRIDE; Q725C4; -.
DR KEGG; lmf:LMOf2365_0049; -.
DR HOGENOM; CLU_037682_1_0_9; -.
DR OMA; GNVACIT; -.
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..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