TADA_AGRFC
ID TADA_AGRFC Reviewed; 152 AA.
AC A9CK16;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Atu0688;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-144 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF GLU-55; ARG-94; PHE-144; PHE-145 AND ARG-149.
RX PubMed=16142903; DOI=10.1021/bi050499f;
RA Elias Y., Huang R.H.;
RT "Biochemical and structural studies of A-to-I editing by tRNA:A34
RT deaminases at the wobble position of transfer RNA.";
RL Biochemistry 44:12057-12065(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 ECO:0000269|PubMed:16142903}.
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 ECO:0000269|PubMed:16142903};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:16142903};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:16142903};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:16142903}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000255|HAMAP-Rule:MF_00972}.
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DR EMBL; AE007869; AAK86497.1; -; Genomic_DNA.
DR PIR; AB2661; AB2661.
DR PIR; H97442; H97442.
DR RefSeq; NP_353712.1; NC_003062.2.
DR RefSeq; WP_010971070.1; NC_003062.2.
DR PDB; 2A8N; X-ray; 1.60 A; A/B=1-144.
DR PDBsum; 2A8N; -.
DR AlphaFoldDB; A9CK16; -.
DR SMR; A9CK16; -.
DR STRING; 176299.Atu0688; -.
DR EnsemblBacteria; AAK86497; AAK86497; Atu0688.
DR GeneID; 66220854; -.
DR KEGG; atu:Atu0688; -.
DR PATRIC; fig|176299.10.peg.684; -.
DR eggNOG; COG0590; Bacteria.
DR HOGENOM; CLU_025810_3_2_5; -.
DR OMA; PCQMCAG; -.
DR PhylomeDB; A9CK16; -.
DR BioCyc; AGRO:ATU0688-MON; -.
DR BRENDA; 3.5.4.33; 200.
DR EvolutionaryTrace; A9CK16; -.
DR Proteomes; UP000000813; Chromosome circular.
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; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..152
FT /note="tRNA-specific adenosine deaminase"
FT /id="PRO_0000423948"
FT DOMAIN 2..111
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 ECO:0000269|PubMed:16142903"
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:16142903"
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:16142903"
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:16142903"
FT MUTAGEN 55
FT /note="E->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16142903"
FT MUTAGEN 94
FT /note="R->A: 220-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:16142903"
FT MUTAGEN 144
FT /note="F->A: 800-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:16142903"
FT MUTAGEN 145
FT /note="F->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:16142903"
FT MUTAGEN 149
FT /note="R->A: 800-fold decrease in activity."
FT /evidence="ECO:0000269|PubMed:16142903"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:2A8N"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:2A8N"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2A8N"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2A8N"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:2A8N"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2A8N"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2A8N"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:2A8N"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2A8N"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:2A8N"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2A8N"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2A8N"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:2A8N"
SQ SEQUENCE 152 AA; 16753 MW; 22E44FDBE8FE8CBD CRC64;
MAERTHFMEL ALVEARSAGE RDEVPIGAVL VLDGRVIARS GNRTRELNDV TAHAEIAVIR
MACEALGQER LPGADLYVTL EPCTMCAAAI SFARIRRLYY GAQDPKGGAV ESGVRFFSQP
TCHHAPDVYS GLAESESAEI LRQFFREKRL DD
