ID   TSAC_MORCB              Reviewed;         204 AA.
AC   D5V9A9;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            Short=TC-AMP synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE            EC=2.7.7.87 {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC {ECO:0000255|HAMAP-Rule:MF_01852};
GN   Name=tsaC {ECO:0000255|HAMAP-Rule:MF_01852}; Synonyms=rimN;
GN   OrderedLocusNames=MCR_1892;
OS   Moraxella catarrhalis (strain BBH18).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=1236608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BBH18;
RX   PubMed=20453089; DOI=10.1128/jb.00121-10;
RA   de Vries S.P., van Hijum S.A., Schueler W., Riesbeck K., Hays J.P.,
RA   Hermans P.W., Bootsma H.J.;
RT   "Genome analysis of Moraxella catarrhalis strain RH4, a human respiratory
RT   tract pathogen.";
RL   J. Bacteriol. 192:3574-3583(2010).
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:0000255|HAMAP-
CC       Rule:MF_01852}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01852};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01852}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01852}.
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DR   EMBL; CP002005; ADG62148.1; -; Genomic_DNA.
DR   RefSeq; WP_013108276.1; NC_014147.1.
DR   AlphaFoldDB; D5V9A9; -.
DR   SMR; D5V9A9; -.
DR   STRING; 1236608.MCR_1892; -.
DR   EnsemblBacteria; ADG62148; ADG62148; MCR_1892.
DR   KEGG; mct:MCR_1892; -.
DR   PATRIC; fig|1236608.7.peg.1921; -.
DR   HOGENOM; CLU_031397_6_0_6; -.
DR   OMA; LVDAFWP; -.
DR   OrthoDB; 1913202at2; -.
DR   Proteomes; UP000000930; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01852; TsaC; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR023535; TC-AMP_synthase.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   PANTHER; PTHR17490:SF8; PTHR17490:SF8; 1.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 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..204
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000403979"
FT   DOMAIN          10..204
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ   SEQUENCE   204 AA;  22159 MW;  1138A50BF6601DA4 CRC64;
     MAGSKQIFGA DELDLVANYL QAGGVLAYPS ESVWGLGCDA FNTDAINQII NLKHRDIGKG
     LIVLTDAAER LKSLIDVSHE TSLLDYMQNF SDEFTHKHSR ALTWLMPIQS SVLPSVLIGS
     HDTLAVRITT HPLLKDLCHA LISPTNPYGF LVSTSCNLSK STPAKNLTQA MGYFGDQIAY
     LDTDGLGFAQ PSCIKDLLAG HILR