TSAC_MYCLE
ID TSAC_MYCLE Reviewed; 220 AA.
AC P45831;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 111.
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 ML1136;
GN OrderedLocusNames=ML1136;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; U15186; AAA63091.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31517.1; -; Genomic_DNA.
DR PIR; T09983; T09983.
DR RefSeq; NP_301830.1; NC_002677.1.
DR AlphaFoldDB; P45831; -.
DR SMR; P45831; -.
DR STRING; 272631.ML1136; -.
DR EnsemblBacteria; CAC31517; CAC31517; CAC31517.
DR KEGG; mle:ML1136; -.
DR PATRIC; fig|272631.5.peg.2058; -.
DR Leproma; ML1136; -.
DR eggNOG; COG0009; Bacteria.
DR HOGENOM; CLU_031397_3_1_11; -.
DR OMA; LVDAFWP; -.
DR Proteomes; UP000000806; 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 Reference proteome; Transferase; tRNA processing.
FT CHAIN 1..220
FT /note="Putative threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000202024"
FT DOMAIN 17..202
FT /note="YrdC-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
SQ SEQUENCE 220 AA; 22697 MW; 5273A389520D66D7 CRC64;
MVRMNEVFDC ADPDQRARGI ASAVAALKGG RLVVMPTDTV YGIGADAFDR AAVAALLSAK
GRGRDMPVGV LVGSWHTIEG LVYTMPDGAR ELIRAFWPGA LSLVVVHAPS LNWDLGDAHG
TVMLRMPLHS VAIELLCEVG PMAVSSANVS GQPAAVDVDG ARGQLGELVG VYLDAGPSAQ
QAASTIVDLT EATPRILRAG PVSVARIAEV LGVVPASLIA