(data stored in ACNUC7421 zone)

SWISSPROT: TSAD_EDWI9

ID   TSAD_EDWI9              Reviewed;         341 AA.
AC   C5BHG1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
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=NT01EI_0527;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR67760.1; -; Genomic_DNA.
DR   RefSeq; WP_015869960.1; NC_012779.2.
DR   SMR; C5BHG1; -.
DR   STRING; 634503.NT01EI_0527; -.
DR   EnsemblBacteria; ACR67760; ACR67760; NT01EI_0527.
DR   GeneID; 7961552; -.
DR   KEGG; eic:NT01EI_0527; -.
DR   PATRIC; fig|634503.3.peg.477; -.
DR   eggNOG; ENOG4105CPM; Bacteria.
DR   eggNOG; COG0533; LUCA.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   OrthoDB; POG091H010B; -.
DR   Proteomes; UP000001485; Chromosome.
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; IPR017860; Peptidase_M22_CS.
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.
DR   PROSITE; PS01016; GLYCOPROTEASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BHG1.
DR   SWISS-2DPAGE; C5BHG1.
KW   Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding;
KW   Reference proteome; Transferase; tRNA processing.
FT   CHAIN         1    341       tRNA N6-adenosine
FT                                threonylcarbamoyltransferase.
FT                                /FTId=PRO_1000215299.
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       300    300       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     272    272       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
SQ   SEQUENCE   341 AA;  36243 MW;  B7A7047D1C28A464 CRC64;
     MRILGIETSC DETGIAIYDD EKGILANQLY SQIKLHADYG GVVPELASRD HVRKTVPLIQ
     AALREADLTP ADLDGVAYTA GPGLVGALLV GATVGRSLAF AWGVPAVPVH HMEGHLLAPM
     LEENPPAFPF VALLVSGGHT QLISVTGIGE YRLLGESIDD AAGEAFDKTA KLLGLDYPGG
     PVLSRMAQQG VPGRFVFPRP MTDRPGLDLS FSGLKTFAAN TIHANGDDAQ TRADIARAFE
     DAVVDTLAIK CRRALDQTGF QRLVMAGGVS ANRALRGRLA QMMQQRGGAV FYARPEFCTD
     NGAMIAYAGM VRLKSGVDAD LSISVRPRWP LAELPPVAAR S
//

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