AGUA_SHEB5
ID AGUA_SHEB5 Reviewed; 370 AA.
AC A3D798;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=Sbal_3130;
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000563; ABN62611.1; -; Genomic_DNA.
DR RefSeq; WP_011847440.1; NC_009052.1.
DR AlphaFoldDB; A3D798; -.
DR SMR; A3D798; -.
DR STRING; 325240.Sbal_3130; -.
DR EnsemblBacteria; ABN62611; ABN62611; Sbal_3130.
DR KEGG; sbl:Sbal_3130; -.
DR HOGENOM; CLU_037682_1_0_6; -.
DR OMA; WCRDHGP; -.
DR Proteomes; UP000001557; 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..370
FT /note="Putative agmatine deiminase"
FT /id="PRO_1000070567"
FT ACT_SITE 361
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
SQ SEQUENCE 370 AA; 40865 MW; 2C0C67ED143575FE CRC64;
MTNANVDATP LTTKPSQDGF YMPAEWAAQQ AVWMIWPYRP DNWRSAGAYA QATFAKVADA
IGGATPVYMG VPKAFLAEAQ KVMPSHVTLV EMDSNDCWAR DTGPTVVVND NGECRGVDWG
FNAWGGHNGG LYFPWDKDEQ VAQQMLKQHG FARYSAPLIL EGGSIHVDGE GTCMTSAECL
LNANRNPELT KEQIEDLLRD YLNVKQFIWL QDGVYMDETD GHIDNMCCFA RPGEVILHWT
DDETDPQYPR SKAALDVLQN TVDAQGRKLK IHLLPQPGPL YCTEEESLGV TEGTGVPRTA
GERLAGSYVN FLITNNRIVF PMLDPATDDI AAQKLQEIFP EYEIIGVPAR EILLGGGNIH
CITQQIPSGK