ID TSAC_ECOUT Reviewed; 190 AA. AC Q1R650; DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 2. DT 19-FEB-2014, entry version 48. DE RecName: Full=Threonylcarbamoyl-AMP synthase; DE Short=TC-AMP synthase; DE EC=2.7.7.87; DE AltName: Full=L-threonylcarbamoyladenylate synthase; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC; GN Name=tsaC; Synonyms=rimN; OrderedLocusNames=UTI89_C3727; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UTI89 / UPEC; RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Catalyzes the conversion of L-threonine, CC bicarbonate/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) CC as the acyladenylate intermediate, with the release of CC pyrophosphate (By similarity). CC -!- CATALYTIC ACTIVITY: L-threonine + ATP + bicarbonate = L- CC threonylcarbamoyladenylate + diphosphate + H(2)O. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily. CC -!- SIMILARITY: Contains 1 YrdC-like domain. CC -!- SEQUENCE CAUTION: CC Sequence=ABE09164.1; Type=Erroneous initiation; 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; CP000243; ABE09164.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_542695.1; NC_007946.1. DR ProteinModelPortal; Q1R650; -. DR SMR; Q1R650; 3-188. DR STRING; 364106.UTI89_C3727; -. DR EnsemblBacteria; ABE09164; ABE09164; UTI89_C3727. DR GeneID; 3990039; -. DR KEGG; eci:UTI89_C3727; -. DR PATRIC; 18456926; VBIEscCol42261_3670. DR eggNOG; COG0009; -. DR HOGENOM; HOG000076163; -. DR KO; K07566; -. DR OMA; FGLGCNP; -. DR OrthoDB; EOG6C5RT4; -. DR ProtClustDB; PRK10634; -. DR BioCyc; ECOL364106:GHPQ-3698-MONOMER; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070526; P:threonylcarbamoyladenosine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.870.10; -; 1. 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 Pfam; PF01300; Sua5_yciO_yrdC; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Nucleotidyltransferase; Transferase; tRNA processing. FT CHAIN 1 190 Threonylcarbamoyl-AMP synthase. FT /FTId=PRO_0000352915. FT DOMAIN 7 190 YrdC-like. 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 //