TADA_STAAM
ID TADA_STAAM Reviewed; 156 AA.
AC Q99W51;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=SAV0558;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC AND RNA,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=16415880; DOI=10.1038/nsmb1047;
RA Losey H.C., Ruthenburg A.J., Verdine G.L.;
RT "Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA
RT in complex with RNA.";
RL Nat. Struct. Mol. Biol. 13:153-159(2006).
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:16415880};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:16415880};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:16415880}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000255|HAMAP-Rule:MF_00972}.
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DR EMBL; BA000017; BAB56720.1; -; Genomic_DNA.
DR PIR; H89823; H89823.
DR RefSeq; WP_000180281.1; NC_002758.2.
DR PDB; 2B3J; X-ray; 2.00 A; A/B/C/D=1-156.
DR PDBsum; 2B3J; -.
DR AlphaFoldDB; Q99W51; -.
DR SMR; Q99W51; -.
DR DIP; DIP-29048N; -.
DR World-2DPAGE; 0002:Q99W51; -.
DR PaxDb; Q99W51; -.
DR EnsemblBacteria; BAB56720; BAB56720; SAV0558.
DR KEGG; sav:SAV0558; -.
DR HOGENOM; CLU_025810_3_2_9; -.
DR OMA; PCQMCAG; -.
DR PhylomeDB; Q99W51; -.
DR BioCyc; SAUR158878:SAV_RS03115-MON; -.
DR BRENDA; 3.5.4.33; 3352.
DR EvolutionaryTrace; Q99W51; -.
DR Proteomes; UP000002481; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; tRNA processing; Zinc.
FT CHAIN 1..156
FT /note="tRNA-specific adenosine deaminase"
FT /id="PRO_0000423949"
FT DOMAIN 2..120
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 55
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT BINDING 53
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:16415880"
FT BINDING 83
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:16415880"
FT BINDING 86
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:16415880"
FT HELIX 2..20
FT /evidence="ECO:0007829|PDB:2B3J"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2B3J"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2B3J"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2B3J"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:2B3J"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2B3J"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2B3J"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2B3J"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2B3J"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2B3J"
FT HELIX 134..150
FT /evidence="ECO:0007829|PDB:2B3J"
SQ SEQUENCE 156 AA; 17090 MW; AABDDD24AF14DC12 CRC64;
MTNDIYFMTL AIEEAKKAAQ LGEVPIGAII TKDDEVIARA HNLRETLQQP TAHAEHIAIE
RAAKVLGSWR LEGCTLYVTL EPCVMCAGTI VMSRIPRVVY GADDPKGGCS GSLMNLLQQS
NFNHRAIVDK GVLKEACSTL LTTFFKNLRA NKKSTN
