TSAD_DEIGD
ID TSAD_DEIGD Reviewed; 333 AA.
AC Q1IZH8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Dgeo_1057;
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000359; ABF45356.1; -; Genomic_DNA.
DR RefSeq; WP_011530193.1; NC_008025.1.
DR AlphaFoldDB; Q1IZH8; -.
DR SMR; Q1IZH8; -.
DR STRING; 319795.Dgeo_1057; -.
DR EnsemblBacteria; ABF45356; ABF45356; Dgeo_1057.
DR KEGG; dge:Dgeo_1057; -.
DR eggNOG; COG0533; Bacteria.
DR HOGENOM; CLU_023208_0_2_0; -.
DR OMA; HLEGHIY; -.
DR OrthoDB; 1257362at2; -.
DR Proteomes; UP000002431; 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; IPR017860; Peptidase_M22_CS.
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; 2.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Iron; Metal-binding; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..333
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000303345"
FT BINDING 118
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 140..144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ SEQUENCE 333 AA; 34077 MW; 803E8893C3CB52B3 CRC64;
MTFPRYILGI DTSCDDTGVG VVELAPDGSV QVRANRVWSQ TVHAQYGGVL PELASREHVE
RIDTVTGDAL AEAGLTVGDL AAVAATSGPG LVGALLVGLM YGKGLAQALN VPFYAAHHLE
GHIFAAASEA DLQAPYLALV VSGGHTHLFD VPREGEYVLV GATRDDAAGE AFDKVARLAG
LGYPGGPAIS EAARRGDPEA VPFKEPLQGQ KGFDFSFSGL KTAALLAHRA GAKPEDLAAG
FERAAVRFLV GTTLRAARAY GRETVVVSGG VAANRALREA FAASPVRAVF PGKGLNTDNG
AMIALAGAAA IRAGRAPSPL SEGAVAYAPL ASV
