AGUA_STRMU
ID AGUA_STRMU Reviewed; 369 AA.
AC Q8DW17; Q6IFZ0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=SMU_264;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP IDENTIFICATION.
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=14996823; DOI=10.1128/jb.186.6.1902-1904.2004;
RA Griswold A.R., Chen Y.-Y.M., Burne R.A.;
RT "Analysis of an agmatine deiminase gene cluster in Streptococcus mutans
RT UA159.";
RL J. Bacteriol. 186:1902-1904(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; AE014133; AAN58033.1; -; Genomic_DNA.
DR EMBL; BK004003; DAA04558.1; -; Genomic_DNA.
DR RefSeq; NP_720727.1; NC_004350.2.
DR RefSeq; WP_002262731.1; NC_004350.2.
DR PDB; 2EWO; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-369.
DR PDBsum; 2EWO; -.
DR AlphaFoldDB; Q8DW17; -.
DR SMR; Q8DW17; -.
DR STRING; 210007.SMU_264; -.
DR BindingDB; Q8DW17; -.
DR ChEMBL; CHEMBL3559648; -.
DR PRIDE; Q8DW17; -.
DR EnsemblBacteria; AAN58033; AAN58033; SMU_264.
DR KEGG; smu:SMU_264; -.
DR PATRIC; fig|210007.7.peg.230; -.
DR eggNOG; COG2957; Bacteria.
DR HOGENOM; CLU_037682_0_0_9; -.
DR OMA; WCRDHGP; -.
DR PhylomeDB; Q8DW17; -.
DR EvolutionaryTrace; Q8DW17; -.
DR Proteomes; UP000002512; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..369
FT /note="Putative agmatine deiminase"
FT /id="PRO_0000194344"
FT ACT_SITE 361
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01841"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 122..128
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 342..347
FT /evidence="ECO:0007829|PDB:2EWO"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:2EWO"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:2EWO"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:2EWO"
SQ SEQUENCE 369 AA; 41837 MW; 568713173C4AA7D7 CRC64;
MAKRIKNTTP KQDGFRMPGE FEKQKQIWML WPWRNDNWRL GAKPAQKAFL EVAEAISEFE
PVSLCVPPLQ YENALARVSE LGSHNIRIIE MTNDDAWIRD CGPTFLVNDK GDLRAVDWEF
NAWGGLVDGL YFPWDQDALV ARKVCEIEGV DSYKTKDFVL EGGSIHVDGE GTVLVTEMCL
LHPSRNPHLT KEDIEDKLKD YLNCVKVLWV KDGIDPYETN GHIDDVACFI RPGEVACIYT
DDKEHPFYQE AKAAYDFLSQ QTDAKGRPLK VHKMCVTKEP CYLQEAATID YVEGSIPREE
GEMAIASYLN FLIVNGGIIL PQYGDENDQL AKQQVQEMFP DRKVVGVRTE EIAYGGGNIH
CITQQQPAT
