ID   TADA_SALTY              Reviewed;         172 AA.
AC   Q7CQ08;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=tRNA-specific adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00972};
DE            EC=3.5.4.33 {ECO:0000255|HAMAP-Rule:MF_00972};
GN   Name=tadA {ECO:0000255|HAMAP-Rule:MF_00972}; OrderedLocusNames=STM2568;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the
CC       wobble position 34 of tRNA(Arg2). {ECO:0000255|HAMAP-Rule:MF_00972}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC         NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC         COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00972};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00972};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00972}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL21462.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL21462.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_461503.1; NC_003197.2.
DR   AlphaFoldDB; Q7CQ08; -.
DR   SMR; Q7CQ08; -.
DR   STRING; 99287.STM2568; -.
DR   PaxDb; Q7CQ08; -.
DR   EnsemblBacteria; AAL21462; AAL21462; STM2568.
DR   GeneID; 1254090; -.
DR   KEGG; stm:STM2568; -.
DR   PATRIC; fig|99287.12.peg.2709; -.
DR   HOGENOM; CLU_025810_3_0_6; -.
DR   OMA; PCQMCAG; -.
DR   PhylomeDB; Q7CQ08; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central.
DR   HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR028883; tRNA_aden_deaminase.
DR   Pfam; PF14437; MafB19-deam; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..172
FT                   /note="tRNA-specific adenosine deaminase"
FT                   /id="PRO_0000171737"
FT   DOMAIN          6..117
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        59
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
SQ   SEQUENCE   172 AA;  19204 MW;  CD34E298DAF45F3F CRC64;
     MSDVELDHEY WMRHALTLAK RAWDEREVPV GAVLVHNHRV IGEGWNRPIG RHDPTAHAEI
     MALRQGGLVL QNYRLLDTTL YVTLEPCVMC AGAMVHSRIG RVVFGARDAK TGAAGSLIDV
     LHHPGMNHRV EIIEGVLRDE CATLLSDFFR MRRQEIKALK KADRAEGAGP AV