(data stored in ACNUC7421 zone)

SWISSPROT: TSAD_PSEAB

ID   TSAD_PSEAB              Reviewed;         341 AA.
AC   Q02TI3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 72.
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=PA14_07570;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ15544.1; -; Genomic_DNA.
DR   RefSeq; WP_003137360.1; NC_008463.1.
DR   ProteinModelPortal; Q02TI3; -.
DR   SMR; Q02TI3; -.
DR   EnsemblBacteria; ABJ15544; ABJ15544; PA14_07570.
DR   KEGG; pau:PA14_07570; -.
DR   HOGENOM; HOG000109568; -.
DR   KO; K01409; -.
DR   OMA; HLEGHIY; -.
DR   Proteomes; UP000000653; 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; 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; Q02TI3.
DR   SWISS-2DPAGE; Q02TI3.
KW   Acyltransferase; Complete proteome; Cytoplasm; Iron; Metal-binding;
KW   Transferase; tRNA processing.
FT   CHAIN         1    341       tRNA N6-adenosine
FT                                threonylcarbamoyltransferase.
FT                                /FTId=PRO_0000303491.
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       304    304       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     276    276       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01445}.
SQ   SEQUENCE   341 AA;  36529 MW;  7F30E8F7636905A0 CRC64;
     MRVLGLETSC DETGVALYDS ERGLLADALF SQIDLHRVYG GVVPELASRD HVKRMLPLIR
     QVLDESGCTP ADIDAIAYTA GPGLVGALLV GASCAQAVAF AWGVPAVGVH HMEGHLLAPM
     LEEQPPRFPF VALLVSGGHT QLVRVDGIGR YQLLGESVDD AAGEAFDKTA KLIGLGYPGG
     PEIARLAERG TPGRFVFPRP MTDRPGLDFS FSGLKTFTLN TWQRCVEAGD DSEQTRCDIA
     LAFQTAVVET LLIKCRRALK QTGLKNLVIA GGVSANQALR SGLEKMLGEM KGQVFYARPR
     FCTDNGAMIA YAGCQRLLAG QHDGPAISVQ PRWPMESLPA V
//

If you have problems or comments...

PBIL Back to PBIL home page