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TSAD_LISMF
ID   TSAD_LISMF              Reviewed;         344 AA.
AC   Q71XT8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
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=LMOf2365_2107;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT04877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017262; AAT04877.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q71XT8; -.
DR   SMR; Q71XT8; -.
DR   KEGG; lmf:LMOf2365_2107; -.
DR   HOGENOM; CLU_023208_0_2_9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISS:JCVI.
DR   GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; ISS:JCVI.
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; Transferase;
KW   tRNA processing.
FT   CHAIN           1..344
FT                   /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT                   /id="PRO_0000303414"
FT   BINDING         119
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         123
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         141..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
FT   BINDING         310
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01445"
SQ   SEQUENCE   344 AA;  36874 MW;  86604B833A599E77 CRC64;
     MGGLMKKNTL ILGIESSCDE TAASVVKNGN EIISSVVASQ IESHKRFGGV VPEIASRHHV
     EQITLVIEEA LKQANVTMDD LDGIAVTEGP GLVGALLIGV NAAKTLAFMH NLPLVGVHHI
     AGHIYANRFE TEFKFPLLSL VVSGGHTELV LMKADNEFEI IGETRDDAAG EAYDKVARTL
     GLAYPGGVQI DKLAKDGEDT FHFPRAMMDE GSFDFSFSGL KSSFINTLHN LRQRGEEPNP
     NDMAASFQAS VVDVLVSKTI RAAKQYDVKQ LLLAGGVAAN QGLRERLIQE VKLELPETEL
     IIPPLALCGD NAAMIAAAGT VSFLQGKRSG FDMNANPGLL LEDI
 
 
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