TADA_AQUAE
ID TADA_AQUAE Reviewed; 151 AA.
AC O67050;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=aq_903;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15677468; DOI=10.1074/jbc.m414541200;
RA Kuratani M., Ishii R., Bessho Y., Fukunaga R., Sengoku T., Shirouzu M.,
RA Sekine S., Yokoyama S.;
RT "Crystal structure of tRNA adenosine deaminase (TadA) from Aquifex
RT aeolicus.";
RL J. Biol. Chem. 280:16002-16008(2005).
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 ECO:0000269|PubMed:15677468};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:15677468};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:15677468}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000255|HAMAP-Rule:MF_00972}.
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DR EMBL; AE000657; AAC07025.1; -; Genomic_DNA.
DR PIR; G70377; G70377.
DR RefSeq; NP_213612.1; NC_000918.1.
DR RefSeq; WP_010880550.1; NC_000918.1.
DR PDB; 1WWR; X-ray; 1.80 A; A/B/C/D=1-151.
DR PDBsum; 1WWR; -.
DR AlphaFoldDB; O67050; -.
DR SMR; O67050; -.
DR STRING; 224324.aq_903; -.
DR EnsemblBacteria; AAC07025; AAC07025; aq_903.
DR KEGG; aae:aq_903; -.
DR PATRIC; fig|224324.8.peg.704; -.
DR eggNOG; COG0590; Bacteria.
DR HOGENOM; CLU_025810_3_2_0; -.
DR InParanoid; O67050; -.
DR OMA; PCQMCAG; -.
DR OrthoDB; 1890883at2; -.
DR BRENDA; 3.5.4.33; 396.
DR EvolutionaryTrace; O67050; -.
DR Proteomes; UP000000798; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..151
FT /note="tRNA-specific adenosine deaminase"
FT /id="PRO_0000171732"
FT DOMAIN 1..111
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 54
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00972,
FT ECO:0000269|PubMed:15677468"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00972,
FT ECO:0000269|PubMed:15677468"
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 ECO:0000269|PubMed:15677468"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:1WWR"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:1WWR"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1WWR"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1WWR"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:1WWR"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1WWR"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1WWR"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1WWR"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:1WWR"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:1WWR"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1WWR"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:1WWR"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:1WWR"
SQ SEQUENCE 151 AA; 17246 MW; 5543DC00B9846D25 CRC64;
MGKEYFLKVA LREAKRAFEK GEVPVGAIIV KEGEIISKAH NSVEELKDPT AHAEMLAIKE
ACRRLNTKYL EGCELYVTLE PCIMCSYALV LSRIEKVIFS ALDKKHGGVV SVFNILDEPT
LNHRVKWEYY PLEEASELLS EFFKKLRNNI I
