TSAD_WOLPP
ID TSAD_WOLPP Reviewed; 336 AA.
AC B3CLX6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, 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=WP0786;
OS Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=570417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wPip;
RX PubMed=18550617; DOI=10.1093/molbev/msn133;
RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.;
RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens group.";
RL Mol. Biol. Evol. 25:1877-1887(2008).
CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning
CC with adenine. Is involved in the transfer of the threonylcarbamoyl
CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37,
CC together with TsaE and TsaB. TsaD likely plays a direct catalytic role
CC in this reaction. {ECO:0000255|HAMAP-Rule:MF_01445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC Evidence={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-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}.
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DR EMBL; AM999887; CAQ54894.1; -; Genomic_DNA.
DR RefSeq; WP_007302199.1; NC_010981.1.
DR AlphaFoldDB; B3CLX6; -.
DR SMR; B3CLX6; -.
DR STRING; 570417.WP0786; -.
DR EnsemblBacteria; CAQ54894; CAQ54894; WP0786.
DR KEGG; wpi:WP0786; -.
DR eggNOG; COG0533; Bacteria.
DR HOGENOM; CLU_023208_0_2_5; -.
DR OMA; HLEGHIY; -.
DR OrthoDB; 1257362at2; -.
DR Proteomes; UP000008814; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01445; TsaD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR022450; TsaD.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Iron; Metal-binding; Transferase;
KW tRNA processing.
FT CHAIN 1..336
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_1000146041"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 133..137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 301
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ SEQUENCE 336 AA; 36694 MW; 97D19966AB35C920 CRC64;
MKTILAIETS CDETAVAIVN SDKQVLANEI LSQVEHKKCG GVIPEIASRA HMKHLSGLIK
SAMEKSNLNF CDLDAIAATS GPGLIGGLII GTMMAKAIAH VTQKPFIAVN HLEAHALVVR
LLYEVEFPFL VLLISGGHCQ FLIAQDVGKY IKLGETLDDS LGEAFDKVAK TLGLSYPGGP
LIEELAKKGD GMRFKLPRAM IKRSGCDLSF SGIKTAVKNL AREFVMSEQD VCDMCASFQE
CISDILLDRV RNAIGIAVSL NIKINDFVIT GGVAANNFLK ERLKKHIDLN VLSPPSNLCT
DNAVMVGWTG IERLQRSYVD SLDFAPRPKW ELEKYY
