TADA_STRP6
ID TADA_STRP6 Reviewed; 171 AA.
AC Q5XE14;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=M6_Spy0214;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR,
RP SUBUNIT, AND FUNCTION.
RX PubMed=17554781; DOI=10.1002/prot.21456;
RA Lee W.H., Kim Y.K., Nam K.H., Priyadarshi A., Lee E.H., Kim E.E.,
RA Jeon Y.H., Cheong C., Hwang K.Y.;
RT "Crystal structure of the tRNA-specific adenosine deaminase from
RT Streptococcus pyogenes.";
RL Proteins 68:1016-1019(2007).
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 ECO:0000269|PubMed:17554781}.
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:17554781};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:17554781};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:17554781}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000255|HAMAP-Rule:MF_00972}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT86349.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000003; AAT86349.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002992549.1; NC_006086.1.
DR PDB; 2NX8; X-ray; 2.00 A; A=1-171.
DR PDBsum; 2NX8; -.
DR AlphaFoldDB; Q5XE14; -.
DR SMR; Q5XE14; -.
DR EnsemblBacteria; AAT86349; AAT86349; M6_Spy0214.
DR GeneID; 57852019; -.
DR KEGG; spa:M6_Spy0214; -.
DR HOGENOM; CLU_025810_3_2_9; -.
DR BRENDA; 3.5.4.33; 5935.
DR EvolutionaryTrace; Q5XE14; -.
DR Proteomes; UP000001167; 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..171
FT /note="tRNA-specific adenosine deaminase"
FT /id="PRO_0000171709"
FT DOMAIN 6..133
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 ECO:0000269|PubMed:17554781"
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 ECO:0000269|PubMed:17554781"
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,
FT ECO:0000269|PubMed:17554781"
FT HELIX 5..24
FT /evidence="ECO:0007829|PDB:2NX8"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2NX8"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2NX8"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2NX8"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:2NX8"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:2NX8"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:2NX8"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:2NX8"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2NX8"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:2NX8"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2NX8"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:2NX8"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2NX8"
FT HELIX 138..164
FT /evidence="ECO:0007829|PDB:2NX8"
SQ SEQUENCE 171 AA; 19261 MW; A4A26E8810580A73 CRC64;
MPYSLEEQTY FMQEALKEAE KSLQKAEIPI GCVIVKDGEI IGRGHNAREE SNQAIMHAEM
MAINEANAHE GNWRLLDTTL FVTIEPCVMC SGAIGLARIP HVIYGASNQK FGGADSLYQI
LTDERLNHRV QVERGLLAAD CANIMQTFFR QGRERKKIAK HLIKEQSDPF D
