TSAC_MYCTU
ID TSAC_MYCTU Reviewed; 217 AA.
AC P9WGC9; L0T985; Q10618;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
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 Rv1301;
GN OrderedLocusNames=Rv1301; ORFNames=MTCY373.21;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44058.1; -; Genomic_DNA.
DR PIR; A70774; A70774.
DR RefSeq; NP_215817.1; NC_000962.3.
DR RefSeq; WP_003898815.1; NZ_NVQJ01000030.1.
DR AlphaFoldDB; P9WGC9; -.
DR SMR; P9WGC9; -.
DR STRING; 83332.Rv1301; -.
DR PaxDb; P9WGC9; -.
DR DNASU; 886970; -.
DR GeneID; 886970; -.
DR KEGG; mtu:Rv1301; -.
DR TubercuList; Rv1301; -.
DR eggNOG; COG0009; Bacteria.
DR OMA; LVDAFWP; -.
DR PhylomeDB; P9WGC9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..217
FT /note="Putative threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000202025"
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