ID A0A290Q848_9LACT Unreviewed; 155 AA.
AC A0A290Q848;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=D9N18_06995 {ECO:0000313|EMBL:MBW9331099.1}, GU335_05965
GN {ECO:0000313|EMBL:QIW57183.1}, GU336_04870
GN {ECO:0000313|EMBL:QIW54933.1};
OS Lactococcus raffinolactis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1366 {ECO:0000313|EMBL:MBW9331099.1, ECO:0000313|Proteomes:UP000709450};
RN [1] {ECO:0000313|EMBL:MBW9331099.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3042 {ECO:0000313|EMBL:MBW9331099.1};
RA Meslier V., Dridi B., Almeida M., Abraham A.-L., Pons N., Renault P.;
RT "Lactococcus raffinolactis, an underestimated dairy Lactococci revealed by
RT genomic and metagenomic analysis.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QIW54933.1, ECO:0000313|Proteomes:UP000501945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lr_19_4S {ECO:0000313|EMBL:QIW57183.1,
RC ECO:0000313|Proteomes:UP000501197}, and Lr_19_5
RC {ECO:0000313|EMBL:QIW54933.1, ECO:0000313|Proteomes:UP000501945};
RA Ybazeta G., Ross M., Brabant-Kirwan D., Saleh M., Dillon J.A., Splinter K.,
RA Nokhbeh R.;
RT "Whole genome sequences of Lactococcus raffinolactis strains isolated from
RT sewage.";
RL Submitted (DEC-2019) 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; RCHZ01000008; MBW9331099.1; -; Genomic_DNA.
DR EMBL; CP047616; QIW54933.1; -; Genomic_DNA.
DR EMBL; CP050534; QIW57183.1; -; Genomic_DNA.
DR RefSeq; WP_061773941.1; NZ_VBTC01000006.1.
DR STRING; 1348633.GCA_001591765_00254; -.
DR GeneID; 47268744; -.
DR OrthoDB; 9802676at2; -.
DR Proteomes; UP000501197; Chromosome.
DR Proteomes; UP000501945; Chromosome.
DR Proteomes; UP000709450; 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 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};
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 6..133
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000259|PROSITE:PS51747"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
SQ SEQUENCE 155 AA; 17362 MW; 1B51AFC7598AFC57 CRC64;
MTFTEEEKAY FMGQALLEAQ KAADHEEVPI GAVIVKDGEI IARSYNAREL HQKATHHAEI
CAIDLANDVV GNWRLIDCAL FVTIEPCVMC SGAISLARLP QVYFGATNPK FGGAVSLYQI
LEDPRLNHRL HVESGILEAE CAQMMQKFFK NRRKK
//