TADA_ECOLI
ID TADA_ECOLI Reviewed; 167 AA.
AC P68398; P30134; Q2MAH1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
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}; Synonyms=yfhC;
GN OrderedLocusNames=b2559, JW2543;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=NWL37;
RX PubMed=1602968; DOI=10.1111/j.1365-2958.1992.tb01540.x;
RA Poulsen L.K., Larsen N.W., Molin S., Andersson P.;
RT "Analysis of an Escherichia coli mutant strain resistant to the cell-
RT killing function encoded by the gef gene family.";
RL Mol. Microbiol. 6:895-905(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Nashimoto H., Saito N.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND CHARACTERIZATION.
RX PubMed=12110595; DOI=10.1093/emboj/cdf362;
RA Wolf J., Gerber A.P., Keller W.;
RT "tadA, an essential tRNA-specific adenosine deaminase from Escherichia
RT coli.";
RL EMBO J. 21:3841-3851(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 2-167 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=16700551; DOI=10.1021/bi0522394;
RA Kim J., Malashkevich V., Roday S., Lisbin M., Schramm V.L., Almo S.C.;
RT "Structural and kinetic characterization of Escherichia coli TadA, the
RT wobble-specific tRNA deaminase.";
RL Biochemistry 45:6407-6416(2006).
CC -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the
CC wobble position 34 of tRNA(Arg2). Essential for cell viability.
CC {ECO:0000255|HAMAP-Rule:MF_00972, ECO:0000269|PubMed:12110595,
CC ECO:0000269|PubMed:16700551}.
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:12110595, ECO:0000269|PubMed:16700551};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:16700551};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:16700551};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.83 uM for tRNA(Arg2) {ECO:0000269|PubMed:16700551};
CC Note=kcat is 13 min(-1). {ECO:0000269|PubMed:16700551};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972,
CC ECO:0000269|PubMed:12110595, ECO:0000269|PubMed:16700551}.
CC -!- DISRUPTION PHENOTYPE: Mutation makes E.coli resistant to the toxic
CC proteins encoded by the gef gene family. {ECO:0000269|PubMed:1602968}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000255|HAMAP-Rule:MF_00972}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA79821.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA10909.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE76735.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA51064.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X72336; CAA51064.1; ALT_INIT; Genomic_DNA.
DR EMBL; D64044; BAA10909.1; ALT_INIT; Genomic_DNA.
DR EMBL; U36841; AAA79821.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75612.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76735.1; ALT_INIT; Genomic_DNA.
DR PIR; F65033; F65033.
DR RefSeq; NP_417054.2; NC_000913.3.
DR RefSeq; WP_001297409.1; NZ_STEB01000011.1.
DR PDB; 1Z3A; X-ray; 2.03 A; A/B=2-167.
DR PDB; 6VPC; EM; 3.20 A; E/F=1-167.
DR PDBsum; 1Z3A; -.
DR PDBsum; 6VPC; -.
DR AlphaFoldDB; P68398; -.
DR SMR; P68398; -.
DR BioGRID; 4261245; 59.
DR IntAct; P68398; 4.
DR STRING; 511145.b2559; -.
DR jPOST; P68398; -.
DR PaxDb; P68398; -.
DR PRIDE; P68398; -.
DR EnsemblBacteria; AAC75612; AAC75612; b2559.
DR EnsemblBacteria; BAE76735; BAE76735; BAE76735.
DR GeneID; 66673553; -.
DR GeneID; 947027; -.
DR KEGG; ecj:JW2543; -.
DR KEGG; eco:b2559; -.
DR PATRIC; fig|1411691.4.peg.4175; -.
DR EchoBASE; EB1346; -.
DR eggNOG; COG0590; Bacteria.
DR HOGENOM; CLU_025810_3_0_6; -.
DR InParanoid; P68398; -.
DR OMA; PCQMCAG; -.
DR PhylomeDB; P68398; -.
DR BioCyc; EcoCyc:EG11372-MON; -.
DR BioCyc; MetaCyc:EG11372-MON; -.
DR BRENDA; 3.5.4.33; 2026.
DR EvolutionaryTrace; P68398; -.
DR PRO; PR:P68398; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006382; P:adenosine to inosine editing; IMP:EcoCyc.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IDA:EcoCyc.
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..167
FT /note="tRNA-specific adenosine deaminase"
FT /id="PRO_0000171733"
FT DOMAIN 6..117
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:16700551"
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:16700551"
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:16700551"
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:16700551"
FT MUTAGEN 53
FT /note="D->E: Resistance to the cell-killing function
FT encoded by the gef gene family."
FT /evidence="ECO:0000269|PubMed:1602968"
FT HELIX 8..24
FT /evidence="ECO:0007829|PDB:1Z3A"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:1Z3A"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1Z3A"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1Z3A"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:1Z3A"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1Z3A"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:1Z3A"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1Z3A"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1Z3A"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1Z3A"
FT HELIX 138..153
FT /evidence="ECO:0007829|PDB:1Z3A"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:6VPC"
SQ SEQUENCE 167 AA; 18718 MW; 6EB59445A86964BC CRC64;
MSEVEFSHEY WMRHALTLAK RAWDEREVPV GAVLVHNNRV IGEGWNRPIG RHDPTAHAEI
MALRQGGLVM QNYRLIDATL YVTLEPCVMC AGAMIHSRIG RVVFGARDAK TGAAGSLMDV
LHHPGMNHRV EITEGILADE CAALLSDFFR MRRQEIKAQK KAQSSTD
