(data stored in ACNUC7421 zone)

SWISSPROT: TADA_BACSU

ID   TADA_BACSU              Reviewed;         161 AA.
AC   P21335;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   11-DEC-2019, entry version 130.
DE   RecName: Full=tRNA-specific adenosine deaminase {ECO:0000255|HAMAP-Rule:MF_00972};
DE            EC=3.5.4.33 {ECO:0000255|HAMAP-Rule:MF_00972};
GN   Name=tadA {ECO:0000255|HAMAP-Rule:MF_00972}; Synonyms=yaaJ;
GN   OrderedLocusNames=BSU00180;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-16.
RC   STRAIN=168;
RX   PubMed=1698458; DOI=10.1016/0167-4781(90)90145-r;
RA   Struck J.C.R., Kretschmer-Kazemi F.R., Schroeder W., Hucho F.,
RA   Toschka H.Y., Erdmann V.A.;
RT   "Characterization of a 17 kDa protein gene upstream from the small
RT   cytoplasmic RNA gene of Bacillus subtilis.";
RL   Biochim. Biophys. Acta 1050:80-83(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Catalyzes the deamination of adenosine to inosine at the
CC       wobble position 34 of tRNA(Arg2). {ECO:0000255|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:0000255|HAMAP-Rule:MF_00972};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00972};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00972}.
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00972}.
DR   EMBL; X52144; CAA36389.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05254.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11794.1; -; Genomic_DNA.
DR   PIR; S11690; S11690.
DR   RefSeq; NP_387899.1; NC_000964.3.
DR   RefSeq; WP_003247140.1; NZ_JNCM01000024.1.
DR   SMR; P21335; -.
DR   STRING; 224308.BSU00180; -.
DR   PaxDb; P21335; -.
DR   PRIDE; P21335; -.
DR   EnsemblBacteria; CAB11794; CAB11794; BSU00180.
DR   GeneID; 937989; -.
DR   KEGG; bsu:BSU00180; -.
DR   PATRIC; fig|224308.179.peg.18; -.
DR   eggNOG; ENOG4108Z6B; Bacteria.
DR   eggNOG; COG0590; LUCA.
DR   HOGENOM; HOG000085050; -.
DR   InParanoid; P21335; -.
DR   KO; K11991; -.
DR   OMA; LEPCQMC; -.
DR   PhylomeDB; P21335; -.
DR   BioCyc; BSUB:BSU00180-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0052718; C:tRNA-specific adenosine-34 deaminase complex; IBA:GO_Central.
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   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; SSF53927; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P21335.
DR   SWISS-2DPAGE; P21335.
KW   Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome;
KW   tRNA processing; Zinc.
FT   CHAIN           1..161
FT                   /note="tRNA-specific adenosine deaminase"
FT                   /id="PRO_0000171705"
FT   DOMAIN          2..120
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT   ACT_SITE        55
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   METAL           53
FT                   /note="Zinc; via pros nitrogen; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   METAL           83
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
FT   METAL           86
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00972"
SQ   SEQUENCE   161 AA;  17752 MW;  3256F31DF6610FBB CRC64;
     MTQDELYMKE AIKEAKKAEE KGEVPIGAVL VINGEIIARA HNLRETEQRS IAHAEMLVID
     EACKALGTWR LEGATLYVTL EPCPMCAGAV VLSRVEKVVF GAFDPKGGCS GTLMNLLQEE
     RFNHQAEVVS GVLEEECGGM LSAFFRELRK KKKAARKNLS E
//

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