ID   TSAC_MYCTO              Reviewed;         217 AA.
AC   P9WGC8; L0T985; Q10618;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Putative threonylcarbamoyl-AMP synthase;
DE            Short=TC-AMP synthase;
DE            EC=2.7.7.87;
DE   AltName: Full=L-threonylcarbamoyladenylate synthase;
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein MT1340;
GN   OrderedLocusNames=MT1340;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2)
CC       and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate
CC       intermediate, with the release of diphosphate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC         threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45602.1; -; Genomic_DNA.
DR   PIR; A70774; A70774.
DR   RefSeq; WP_003898815.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WGC8; -.
DR   SMR; P9WGC8; -.
DR   PRIDE; P9WGC8; -.
DR   EnsemblBacteria; AAK45602; AAK45602; MT1340.
DR   KEGG; mtc:MT1340; -.
DR   PATRIC; fig|83331.31.peg.1447; -.
DR   HOGENOM; CLU_031397_3_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00057; TIGR00057; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW   Transferase; tRNA processing.
FT   CHAIN           1..217
FT                   /note="Putative threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000428384"
FT   DOMAIN          14..199
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
SQ   SEQUENCE   217 AA;  22571 MW;  F3FB7ECBE80C3FEE CRC64;
     MTETFDCADP EQRSRGIVSA VGAIKAGQLV VMPTDTVYGI GADAFDSSAV AALLSAKGRG
     RDMPVGVLVG SWHTIEGLVY SMPDGARELI RAFWPGALSL VVVQAPSLQW DLGDAHGTVM
     LRMPLHPVAI ELLREVGPMA VSSANISGHP PPVDAEQARS QLGDHVAVYL DAGPSEQQAG
     STIVDLTGAT PRVLRPGPVS TERIAEVLGV DAASLFG