ID L0F3U1_DESDL Unreviewed; 148 AA.
AC L0F3U1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 OrderedLocusNames=Desdi_0012 {ECO:0000313|EMBL:AGA67588.1};
OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA67588.1, ECO:0000313|Proteomes:UP000010797};
RN [1] {ECO:0000313|Proteomes:UP000010797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Boon N., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL Submitted (FEB-2012) 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|ARBA:ARBA00001103, ECO:0000256|HAMAP-
CC 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|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00972}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000256|ARBA:ARBA00010669}.
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DR EMBL; CP003344; AGA67588.1; -; Genomic_DNA.
DR RefSeq; WP_015260595.1; NC_019903.1.
DR AlphaFoldDB; L0F3U1; -.
DR STRING; 871963.Desdi_0012; -.
DR KEGG; ddl:Desdi_0012; -.
DR eggNOG; COG0590; Bacteria.
DR HOGENOM; CLU_025810_3_2_9; -.
DR OrthoDB; 9802676at2; -.
DR Proteomes; UP000010797; 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 CDD; cd01285; nucleoside_deaminase; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
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 PANTHER; PTHR11079:SF179; CYTOSINE DEAMINASE; 1.
DR PANTHER; PTHR11079; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000010797};
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 1..112
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 148 AA; 16224 MW; A0B3AD67634119F3 CRC64;
MSHQKWMSLA LEEAQLAFEQ GEVPIGAVVV HNNQVIAKAH NEKELRQDPT AHAEVLAVQR
ATQALGVWRL SEATLYVTLE PCPMCAGALV QARLKSLVFG AADLKGGAVG SVTNVLDVNR
WNHRVEVVAG ILEDECAQIL KDFFKKLR
//