TSAC_ALCBS
ID TSAC_ALCBS Reviewed; 182 AA.
AC Q0VTD8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=ABO_0134;
OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS SK2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=393595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX PubMed=16878126; DOI=10.1038/nbt1232;
RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA Weidner S., Kaiser O., Golyshin P.N.;
RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT Alcanivorax borkumensis.";
RL Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL15582.1; -; Genomic_DNA.
DR RefSeq; WP_011587432.1; NC_008260.1.
DR AlphaFoldDB; Q0VTD8; -.
DR SMR; Q0VTD8; -.
DR STRING; 393595.ABO_0134; -.
DR EnsemblBacteria; CAL15582; CAL15582; ABO_0134.
DR KEGG; abo:ABO_0134; -.
DR eggNOG; COG0009; Bacteria.
DR HOGENOM; CLU_031397_6_0_6; -.
DR OMA; LVDAFWP; -.
DR OrthoDB; 1913202at2; -.
DR Proteomes; UP000008871; 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 TIGRFAMs; TIGR00057; TIGR00057; 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..182
FT /note="Threonylcarbamoyl-AMP synthase"
FT /id="PRO_0000352897"
FT DOMAIN 2..182
FT /note="YrdC-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01852"
SQ SEQUENCE 182 AA; 19942 MW; B584EC76504CC731 CRC64;
MNQHLLSAAQ IIQEGGVVAY PTESVYGLGC DPFNRNAVMQ LLAIKHRPVS KGLILIGESL
AQLAPYLHLN EQQSAQLEKK WPAPITYLVD ASDRLPAWVR GEHRKVAVRV PDHPLARQLC
QLAGQPIIST SANISGRPAA RNRYQVARQL GNQLDFIVSG ACDRAAKPST IIDLESGRIL
RP
