(data stored in SCRATCH3701 zone)

SWISSPROT: AGUA1_LISMO

ID   AGUA1_LISMO             Reviewed;         363 AA.
AC   Q8YAS5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 81.
DE   RecName: Full=Putative agmatine deiminase 1 {ECO:0000255|HAMAP-Rule:MF_01841};
DE            EC=3.5.3.12 {ECO:0000255|HAMAP-Rule:MF_01841};
DE   AltName: Full=Agmatine iminohydrolase 1 {ECO:0000255|HAMAP-Rule:MF_01841};
GN   Name=aguA1 {ECO:0000255|HAMAP-Rule:MF_01841}; OrderedLocusNames=lmo0038;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AL591973; CAC98253.1; -; Genomic_DNA.
DR   PIR; AG1079; AG1079.
DR   RefSeq; NP_463571.1; NC_003210.1.
DR   RefSeq; WP_010989327.1; NC_003210.1.
DR   SMR; Q8YAS5; -.
DR   STRING; 169963.lmo0038; -.
DR   PaxDb; Q8YAS5; -.
DR   EnsemblBacteria; CAC98253; CAC98253; CAC98253.
DR   GeneID; 985162; -.
DR   KEGG; lmo:lmo0038; -.
DR   PATRIC; fig|169963.11.peg.39; -.
DR   eggNOG; ENOG4105DWY; Bacteria.
DR   eggNOG; COG2957; LUCA.
DR   KO; K10536; -.
DR   OMA; KQHGSLH; -.
DR   PhylomeDB; Q8YAS5; -.
DR   BioCyc; LMON169963:LMO0038-MONOMER; -.
DR   Proteomes; UP000000817; 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;
DR   PRODOM; Q8YAS5.
DR   SWISS-2DPAGE; Q8YAS5.
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..363
FT                   /note="Putative agmatine deiminase 1"
FT                   /id="PRO_0000194333"
FT   ACT_SITE        356
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ   SEQUENCE   363 AA;  40956 MW;  273E9690E00ADC21 CRC64;
     MRTIDSSSKK DGFRMPGEFE KHAGCYIIWP ERPDNWRLGA KPAQKAFVDV ATAISHFEPV
     TVVASSSQYV NARYMLSDEI RVVEMDNDDA WVRDSGPTFV VNDSGDVRGV DWSFNSWGGL
     VDGLYFPWDK DDQVAQKICE LERKDRYRLA DFVLEGGSIH VDGEGTLVTT EECLLSEGRN
     PQLSKQQIEM VLKEYLNLEK IIWLKRGIYL DETNGHVDNI FNYVRPGVVA LAWTDDETDP
     QYEISKECFD ILSNETDAKG RKLEVHKINV PKPILITDEE SKGVDAVEGT LPREEGDRLA
     ASYINYYTAN GGVIFPLFGD PNDELAREKL QQLYPNCEVV GVKAREILLG GGNIHCITQQ
     VPR
//

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