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Database: UniProt
Entry: W0RIS5_9BACT
LinkDB: W0RIS5_9BACT
Original site: W0RIS5_9BACT 
ID   W0RIS5_9BACT            Unreviewed;       168 AA.
AC   W0RIS5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=J421_3139 {ECO:0000313|EMBL:AHG90676.1};
OS   Gemmatirosa kalamazoonensis.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatirosa.
OX   NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG90676.1, ECO:0000313|Proteomes:UP000019151};
RN   [1] {ECO:0000313|EMBL:AHG90676.1, ECO:0000313|Proteomes:UP000019151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS708 {ECO:0000313|EMBL:AHG90676.1,
RC   ECO:0000313|Proteomes:UP000019151};
RX   PubMed=24699952;
RA   Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA   Fawaz M.N., Korlach J., Tsai Y.C.;
RT   "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT   kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT   Phylum.";
RL   Genome Announc. 2:e00226-14(2014).
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; CP007128; AHG90676.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0RIS5; -.
DR   STRING; 861299.J421_3139; -.
DR   KEGG; gba:J421_3139; -.
DR   PATRIC; fig|861299.3.peg.3190; -.
DR   eggNOG; COG0590; Bacteria.
DR   HOGENOM; CLU_025810_3_2_0; -.
DR   InParanoid; W0RIS5; -.
DR   OrthoDB; 9802676at2; -.
DR   Proteomes; UP000019151; 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; CYTOSINE DEAMINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR11079:SF179; TRNA(ADENINE(34)) DEAMINASE, CHLOROPLASTIC; 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:UP000019151};
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          4..126
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   ACT_SITE        57
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT   BINDING         55
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"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
SQ   SEQUENCE   168 AA;  18251 MW;  0EC4F8B7504B3C34 CRC64;
     MRDTDDEHWM REALARARDA ARDAEVPVGA VIVRDGELLA AAANRTLRDQ DPTAHAETLA
     IRAAAASLGR WRLDDCTLVV TLEPCAMCAG AIVLARLARV VFGAWDDKAG MAGSVGDLLR
     HPRLNHRPQV RGGVLQEECG AMLRDFFAAR RGRIDAPLEG PFTDQSAR
//
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