TSAC_XANOP
ID TSAC_XANOP Reviewed; 187 AA.
AC B2SL46;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=PXO_04048;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000967; ACD57323.1; -; Genomic_DNA.
DR RefSeq; WP_011257486.1; NC_010717.2.
DR AlphaFoldDB; B2SL46; -.
DR SMR; B2SL46; -.
DR STRING; 360094.PXO_04048; -.
DR EnsemblBacteria; ACD57323; ACD57323; PXO_04048.
DR KEGG; xop:PXO_04048; -.
DR eggNOG; COG0009; Bacteria.
DR HOGENOM; CLU_031397_6_0_6; -.
DR OMA; LVDAFWP; -.
DR OrthoDB; 1913202at2; -.
DR Proteomes; UP000001740; 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..187
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000353016"
FT DOMAIN 4..187
FT /note="YrdC-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ SEQUENCE 187 AA; 19884 MW; 119C3E3FF80DCBCE CRC64;
MTHILTLDNA VATLTQGGVI AYPTEAVWGL GCDPRQEAAV LRLLEIKRRP VDKGVIVVTS
RVDVLRDWVD IDALAPARRQ DVLASWPGPH TWILPVTARA PRWVTGEHDG LAVRISAHPV
VAALCAAWGA PLVSTSANLA GEPPARSRAA LEPALLATID GVVDGEVGAL AQPTRIRDAR
SGQILRD
