ID A0A807M7X0_9BACI Unreviewed; 160 AA. AC A0A807M7X0; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 14-DEC-2022, entry version 5. 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=BZ167_09625 {ECO:0000313|EMBL:AQP96228.1}; OS Bacillus sp. 275. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1941347 {ECO:0000313|EMBL:AQP96228.1, ECO:0000313|Proteomes:UP000188970}; RN [1] {ECO:0000313|EMBL:AQP96228.1, ECO:0000313|Proteomes:UP000188970} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=275 {ECO:0000313|EMBL:AQP96228.1, RC ECO:0000313|Proteomes:UP000188970}; RA Gong G., Kim S., Um Y.; RT "Complete genome of Bacillus sp. 275."; RL Submitted (FEB-2017) 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 --------------------------------------------------------------------------- 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; CP019626; AQP96228.1; -; Genomic_DNA. DR RefSeq; WP_015416644.1; NZ_CP019626.1. DR AlphaFoldDB; A0A807M7X0; -. DR Proteomes; UP000188970; 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; Cytidine deaminase-like; 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}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_00972}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00972}. FT DOMAIN 1..119 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" FT ACT_SITE 54 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972" SQ SEQUENCE 160 AA; 17929 MW; 8B0784D70492133F CRC64; MNDEYYMREA IKEAKKAEAK GEVPIGAVLV LHDEIVARAH NLRETEQRSL AHAEMLAIDE ACCKLGTWRL EDAVLYVTLE PCPMCAGAVV LSRVDKVVFG AFDPKGGCTG TLMNLLQEER FNHQAEVVSG VLGEECGEML SAFFRKLRRQ KKDMRKKLSE //