TSAD_THEMA
ID TSAD_THEMA Reviewed; 327 AA.
AC Q9WXZ2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=TM_0145;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS), AND SUBUNIT.
RX PubMed=29741707; DOI=10.1093/nar/gky323;
RA Missoury S., Plancqueel S., Li de la Sierra-Gallay I., Zhang W., Liger D.,
RA Durand D., Dammak R., Collinet B., van Tilbeurgh H.;
RT "The structure of the TsaB/TsaD/TsaE complex reveals an unexpected
RT mechanism for the bacterial t6A tRNA-modification.";
RL Nucleic Acids Res. 46:5850-5860(2018).
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 -!- SUBUNIT: Forms an hexamer composed of two TsaB, TsaD and TsaE trimers.
CC {ECO:0000269|PubMed:29741707}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000512; AAD35238.1; -; Genomic_DNA.
DR PIR; G72411; G72411.
DR RefSeq; NP_227960.1; NC_000853.1.
DR RefSeq; WP_004082750.1; NZ_CP011107.1.
DR PDB; 6N9A; X-ray; 2.50 A; D=1-327.
DR PDB; 6S84; X-ray; 2.89 A; A/D=1-327.
DR PDBsum; 6N9A; -.
DR PDBsum; 6S84; -.
DR AlphaFoldDB; Q9WXZ2; -.
DR SMR; Q9WXZ2; -.
DR STRING; 243274.THEMA_04075; -.
DR DNASU; 896976; -.
DR EnsemblBacteria; AAD35238; AAD35238; TM_0145.
DR KEGG; tma:TM0145; -.
DR eggNOG; COG0533; Bacteria.
DR InParanoid; Q9WXZ2; -.
DR OMA; HLEGHIY; -.
DR OrthoDB; 1257362at2; -.
DR Proteomes; UP000008183; 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; 2.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Iron; Metal-binding;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..327
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000303595"
FT BINDING 109
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 132..136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:6N9A"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 83..100
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6S84"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:6S84"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 228..254
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:6N9A"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6N9A"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:6N9A"
SQ SEQUENCE 327 AA; 35628 MW; F8373046AED4858C CRC64;
MRVLGIETSC DETAVAVLDD GKNVVVNFTV SQIEVHQKFG GVVPEVAARH HLKNLPILLK
KAFEKVPPET VDVVAATYGP GLIGALLVGL SAAKGLAISL EKPFVGVNHV EAHVQAVFLA
NPDLKPPLVV LMVSGGHTQL MKVDEDYSME VLGETLDDSA GEAFDKVARL LGLGYPGGPV
IDRVAKKGDP EKYSFPRPML DDDSYNFSFA GLKTSVLYFL QREKGYKVED VAASFQKAVV
DILVEKTFRL ARNLGIRKIA FVGGVAANSM LREEVRKRAE RWNYEVFFPP LELCTDNALM
VAKAGYEKAK RGMFSPLSLN ADPNLNV
