TSAC_STRMK
ID TSAC_STRMK Reviewed; 186 AA.
AC B2FIS1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
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=Smlt4185;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ47576.1; -; Genomic_DNA.
DR AlphaFoldDB; B2FIS1; -.
DR SMR; B2FIS1; -.
DR STRING; 522373.Smlt4185; -.
DR EnsemblBacteria; CAQ47576; CAQ47576; Smlt4185.
DR KEGG; sml:Smlt4185; -.
DR eggNOG; COG0009; Bacteria.
DR HOGENOM; CLU_031397_6_0_6; -.
DR OMA; LVDAFWP; -.
DR Proteomes; UP000008840; 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..186
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000352998"
FT DOMAIN 3..186
FT /note="YrdC-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ SEQUENCE 186 AA; 19843 MW; E863268FA8D4366F CRC64;
MKELTLDSAV ATLRAGGVIA YPTEAVWGLG CDPSHEAAVH MVLRLKQRPI EKGMILVAAD
LAQLEGWVRL QALPDARQRA VLASWPGANT WILPAGPRAQ PWVTGEHSGI AVRISAHPLV
AELCRAWGGP LVSTSANLAG EPPARRREEL DPRLLRLLDG ILDGETGGLA QPTPIRDALS
GNVLRS