AC   MF_01852;
DC   Protein; auto
TR   HAMAP; MF_01852; -; 1; level=0
XX
Names: TsaC
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ID   TSAC
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=tRNA threonylcarbamoyladenosine biosynthesis protein TsaC;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaC;
GN   Name=tsaC;
XX
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.
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SUA5 family. TsaC subfamily.
XX
DR   PROSITE; PS51163; YRDC; 1; trigger=yes
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1; trigger=no
DR   NCBIfam; TIGR00057; TIGR00057; 1; trigger=no
XX
KW   ATP-binding
KW   Cytoplasm
KW   Nucleotide-binding
KW   Nucleotidyltransferase
KW   Transferase
KW   tRNA processing
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GO   GO:0005524; F:ATP binding
GO   GO:0016779; F:nucleotidyltransferase activity
GO   GO:0002949; P:tRNA threonylcarbamoyladenosine modification
GO   GO:0005737; C:cytoplasm
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FT   None
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Size: 175-214;
Related: None;
Template: P45748;
Scope:
 Bacteria; Betaproteobacteria
 Bacteria; Gammaproteobacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: The well-known t(6)A modification appears to be a hydrolyzed artifact of natural
 cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in E.coli,
 B.subtilis and many other species including fungi and plants (PubMed:23242255). In these
 species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction
 catalyzed by TcdA.
XX
# Revision 1.14 2023/06/01
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