(data stored in ACNUC7421 zone)

SWISSPROT: TSAD_PARXL

ID   TSAD_PARXL              Reviewed;         342 AA.
AC   Q13RW9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 79.
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE            Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000255|HAMAP-Rule:MF_01445};
GN   Name=tsaD {ECO:0000255|HAMAP-Rule:MF_01445}; Synonyms=gcp;
GN   OrderedLocusNames=Bxeno_B0202; ORFNames=Bxe_B2825;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group
CC       on adenosine at position 37 (t(6)A37) in tRNAs that read codons
CC       beginning with adenine. Is involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the
CC       N6 group of A37, together with TsaE and TsaB. TsaD likely plays a
CC       direct catalytic role in this reaction. {ECO:0000255|HAMAP-
CC       Rule:MF_01445}.
CC   -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in
CC       tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01445};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01445};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445}.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01445}.
DR   EMBL; CP000271; ABE33170.1; -; Genomic_DNA.
DR   RefSeq; WP_011490546.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13RW9; -.
DR   SMR; Q13RW9; -.
DR   STRING; 266265.Bxe_B2825; -.
DR   EnsemblBacteria; ABE33170; ABE33170; Bxe_B2825.
DR   GeneID; 4006576; -.
DR   KEGG; bxb:DR64_5154; -.
DR   KEGG; bxe:Bxe_B2825; -.
DR   PATRIC; fig|266265.5.peg.4868; -.
DR   eggNOG; ENOG4105CPM; Bacteria.
DR   eggNOG; COG0533; LUCA.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; POG091H010B; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:InterPro.
DR   HAMAP; MF_01445; TsaD; 1.
DR   InterPro; IPR000905; Gcp-like_dom.
DR   InterPro; IPR017861; KAE1/TsaD.
DR   InterPro; IPR022450; TsaD.
DR   Pfam; PF00814; Peptidase_M22; 1.
DR   PRINTS; PR00789; OSIALOPTASE.
DR   TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR   TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13RW9.
DR   SWISS-2DPAGE; Q13RW9.
KW   Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN         1    342       tRNA N6-adenosine
FT                                threonylcarbamoyltransferase.
FT                                /FTId=PRO_0000303308.
FT   REGION      134    138       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
FT   METAL       111    111       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   METAL       115    115       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   METAL       303    303       Iron. {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   BINDING     167    167       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
FT   BINDING     180    180       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01445}.
FT   BINDING     275    275       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
SQ   SEQUENCE   342 AA;  36130 MW;  4B30656A3C31632B CRC64;
     MLVLGIESSC DETGLALYDT ERGLLAHALH SQIAMHREYG GVVPELASRD HIRRALPLLE
     EVMERAGTAA GDIDAIAYTQ GPGLAGALLV GASVANALAM AWDKPTIGIH HLEGHLLSPL
     LVDEPPPFPF VALLVSGGHT QLMRVTDVGV YETLGETLDD AAGEAFDKTA KLLGLGYPGG
     PEVSRMAEFG TPGAVVLPRP MLHSGDLDFS FSGLKTAVLT HAKKLGGANI CEQAKADLAR
     GFVDAAVEVL AAKSLAALKK TGLNRLVVAG GVGANRQLRE ALSAAAKKRN FYVHYPDLSL
     CTDNGAMIAL AGALRLQRWP DQSGKDYAFT VKPRWDLTSL AR
//

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