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TSAC_SHIB3
ID   TSAC_SHIB3              Reviewed;         190 AA.
AC   B2U2Q0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   25-MAY-2022, entry version 64.
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=SbBS512_E3667;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACD09838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP001063; ACD09838.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001297709.1; NC_010658.1.
DR   AlphaFoldDB; B2U2Q0; -.
DR   SMR; B2U2Q0; -.
DR   STRING; 344609.SbBS512_E3667; -.
DR   EnsemblBacteria; ACD09838; ACD09838; SbBS512_E3667.
DR   GeneID; 66672824; -.
DR   KEGG; sbc:SbBS512_E3667; -.
DR   HOGENOM; CLU_031397_6_0_6; -.
DR   Proteomes; UP000001030; 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   Transferase; tRNA processing.
FT   CHAIN           1..190
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000352991"
FT   DOMAIN          7..190
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ   SEQUENCE   190 AA;  20641 MW;  83AE702A6268E3D1 CRC64;
     MNNNLQGDAI AAAIDVLNEE RVIAYPTEAV FGVGCDPDSE TAVMRLLELK QRPVDKGLIL
     IAANYEQLKP YIDDTMLTDA QRETIFSRWP GPVTFVFPAP ATTPRWLTGR FDSLAVRVTD
     HPLVVALCQA YGKPLVSTSA NLSGLPPCRT VDEVRAQFGA AFPVVPGETG GRLNPSEIRD
     ALTGELFRQG
 
 
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