ID   Q9JZR1_NEIMB            Unreviewed;       239 AA.
AC   Q9JZR1;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=NMB0933 {ECO:0000313|EMBL:AAF41340.1};
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF41340.1, ECO:0000313|Proteomes:UP000000425};
RN   [1] {ECO:0000313|EMBL:AAF41340.1, ECO:0000313|Proteomes:UP000000425}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58 {ECO:0000313|EMBL:AAF41340.1,
RC   ECO:0000313|Proteomes:UP000000425};
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L.,
RA   White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A.,
RA   Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H., Qin H., Vamathevan J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; Evidence={ECO:0000256|HAMAP-
CC         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; AE002098; AAF41340.1; -; Genomic_DNA.
DR   PIR; H81141; H81141.
DR   RefSeq; NP_273972.1; NC_003112.2.
DR   RefSeq; WP_002225332.1; NC_003112.2.
DR   AlphaFoldDB; Q9JZR1; -.
DR   STRING; 122586.NMB0933; -.
DR   PaxDb; 122586-NMB0933; -.
DR   DNASU; 903054; -.
DR   KEGG; nme:NMB0933; -.
DR   PATRIC; fig|122586.8.peg.1182; -.
DR   HOGENOM; CLU_025810_2_1_4; -.
DR   InParanoid; Q9JZR1; -.
DR   OrthoDB; 9802676at2; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central.
DR   CDD; cd01285; nucleoside_deaminase; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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; IPR007077; TfoX_C.
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   Pfam; PF04994; TfoX_C; 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:UP000000425};
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          90..223
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   ACT_SITE        143
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00972"
SQ   SEQUENCE   239 AA;  25988 MW;  AF3444A8C60438FE CRC64;
     MLTTPPLAPK TVAALHRLGI RTLEELRQNG SVKAFLLLKA SGLTLTKSTL WQLESLLDGT
     PPQEMSQAHK ARLLAELKNH PPVAAFPPQE EMEHFMCEAL RQAEQSSADG EIPVGAVIVS
     DGKIIASAHN TCIADCNVSR HAEINALAQA GREIQNYRLD GCDIYITLEP CAMCASALIQ
     ARIRRVIYGA AEPKTGAAGS IVNLFADKRL NTHTAIRGGI LQEECRAVLS RFFQNKRKG
//