ID   TADA_BUCAI              Reviewed;         161 AA.
AC   P57343;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=BU255;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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}.
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DR   EMBL; BA000003; BAB12965.1; -; Genomic_DNA.
DR   RefSeq; NP_240079.1; NC_002528.1.
DR   RefSeq; WP_010896028.1; NC_002528.1.
DR   AlphaFoldDB; P57343; -.
DR   SMR; P57343; -.
DR   STRING; 107806.10038930; -.
DR   EnsemblBacteria; BAB12965; BAB12965; BAB12965.
DR   KEGG; buc:BU255; -.
DR   PATRIC; fig|107806.10.peg.265; -.
DR   eggNOG; COG0590; Bacteria.
DR   HOGENOM; CLU_025810_3_0_6; -.
DR   OMA; PCQMCAG; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IEA:UniProtKB-UniRule.
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..161
FT                   /note="tRNA-specific adenosine deaminase"
FT                   /id="PRO_0000171729"
FT   DOMAIN          4..116
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        57
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
SQ   SEQUENCE   161 AA;  18663 MW;  018DE825D8D8D7CC CRC64;
     MKYEKDKNWM KIALKYAYYA KEKGEIPIGA ILVFKERIIG IGWNSSISKN DPTAHAEIIA
     LRGAGKKIKN YRLLNTTLYV TLQPCIMCCG AIIQSRIKRL VFGANCNSSD HRFSLKNLFC
     DPQKDYKLDI KKNVMQRECS DILINFFQKK RKNKIHICKK I