ID A0A1X3K9F6_ECOLX Unreviewed; 178 AA. AC A0A1X3K9F6; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 02-JUN-2021, entry version 10. DE RecName: Full=tRNA-specific adenosine deaminase {ECO:0000256|HAMAP-Rule:MF_00972}; DE EC=3.5.4.33 {ECO:0000256|HAMAP-Rule:MF_00972}; GN Name=tadA {ECO:0000256|HAMAP-Rule:MF_00972}; GN ORFNames=EARG_02876 {ECO:0000313|EMBL:OSL43931.1}; OS Escherichia coli H461. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=656403 {ECO:0000313|EMBL:OSL43931.1, ECO:0000313|Proteomes:UP000193714}; RN [1] {ECO:0000313|EMBL:OSL43931.1, ECO:0000313|Proteomes:UP000193714} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H461 {ECO:0000313|EMBL:OSL43931.1, RC ECO:0000313|Proteomes:UP000193714}; RG The Broad Institute Genome Sequencing Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q., RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D., RA Larson L., Mehta T., Park D., Pearson M., Richards J., Roberts A., Saif S., RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.; RT "The Genome Sequence of Escherichia coli H461."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the CC wobble position 34 of tRNA(Arg2). {ECO:0000256|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:0000256|HAMAP-Rule:MF_00972}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00972}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00972}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00972}. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000256|HAMAP-Rule:MF_00972}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OSL43931.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ADJV01000020; OSL43931.1; -; Genomic_DNA. DR RefSeq; WP_001298403.1; NZ_ADJV01000020.1. DR EnsemblBacteria; OSL43931; OSL43931; EARG_02876. DR GeneID; 61731465; -. DR Proteomes; UP000193714; Unassembled WGS sequence. 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 3: Inferred from homology; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00972}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00972}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00972}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00972}. FT DOMAIN 17..128 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" FT ACT_SITE 70 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" FT METAL 68 FT /note="Zinc; via pros nitrogen; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" FT METAL 98 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" FT METAL 101 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" SQ SEQUENCE 178 AA; 20044 MW; 3BB843A4FD60BA9B CRC64; MRRAFITGVF FLSEVEFSHE YWMRHAMTLA KRAWDEREVP VGAVLVHNNR VIGEGWNRPI GRHDPTAHAE IMALRQGGLV MQNYRLIDAT LYVTLEPCVM CAGAMIHSRI GRVVFGARDA KTGAAGSLMD VLHHPGMNHR VEITEGILAD ECAALLSDFF RMRRQEIKAQ KKAQSSTD //