AC   MF_01886;
DC   Protein; auto
TR   HAMAP; MF_01886; -; 1; level=0
XX
Names: tRNA_acetyltr_TmcA
XX
ID   TMCA
DE   RecName: Full=tRNA(Met) cytidine acetyltransferase TmcA;
DE            EC=2.3.1.193;
GN   Name=tmcA;
XX
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at
CC       the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl
CC       donor and ATP (or GTP).
case <OC:Thermococcales>
CC   -!- FUNCTION: Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) sites
CC       in rRNA, tRNA, mRNA and non-coding (nc)RNA, almost always on the
CC       middle C of a CCG motif. In hyperthermophiles more acetylation is seen
CC       at higher temperatures.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(34) in elongator tRNA(Met) + acetyl-CoA + ATP + H2O =
CC         N(4)-acetylcytidine(34) in elongator tRNA(Met) + ADP + phosphate +
CC         CoA + H(+); Xref=Rhea:RHEA:43788, Rhea:RHEA-COMP:10693, Rhea:RHEA-
CC         COMP:10694, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC         EC=2.3.1.193;
case <OC:Thermococcales>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in RNA + acetyl-CoA + ATP + H2O = an N(4)-
CC         acetylcytidine in RNA + ADP + phosphate + CoA + H(+);
CC         Xref=Rhea:RHEA:82211, Rhea:RHEA-COMP:15704, Rhea:RHEA-COMP:19834,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in tRNA + acetyl-CoA + ATP + H2O = an N(4)-
CC         acetylcytidine in tRNA + ADP + phosphate + CoA + H(+);
CC         Xref=Rhea:RHEA:53876, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:13671,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in mRNA + acetyl-CoA + ATP + H2O = an N(4)-
CC         acetylcytidine in mRNA + ADP + phosphate + CoA + H(+);
CC         Xref=Rhea:RHEA:58480, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15146,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:74900, ChEBI:CHEBI:82748, ChEBI:CHEBI:456216;
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the TmcA family.
XX
DR   PROSITE; PS51186; GNAT; 1; trigger=yes
DR   Pfam; PF08351; DUF1726; 1; trigger=no
DR   Pfam; PF05127; DUF699; 1; trigger=no
DR   Pfam; PF00583; Acetyltransf_1; 1; trigger=no
XX
KW   Acyltransferase
KW   ATP-binding
KW   Cytoplasm
KW   Nucleotide-binding
case <OC:Thermococcales>
KW   rRNA processing
KW   rRNA-binding
end case
KW   RNA-binding
KW   Transferase
KW   tRNA processing
KW   tRNA-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0000049; F:tRNA binding
GO   GO:0051392; F:tRNA cytidine N4-acetyltransferase activity
GO   GO:0051391; P:tRNA acetylation
GO   GO:0002101; P:tRNA wobble cytosine modification
GO   GO:0005737; C:cytoplasm
case <OC:Thermococcales>
GO   GO:1990882; P:rRNA acetylation
end case
XX
FT   From: TMCA_ECOLI (P76562)
FT   BINDING         174..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: G-A
FT   BINDING         202..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: G-R-G-K-S-A-L-A-G-Q
FT   BINDING         461..463
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT   Optional; Condition: [IV]-A-[VT]
FT   BINDING         468..474
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT   Optional; Condition: Q-R-E-G-T-G-R
FT   BINDING         180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: Q
FT   BINDING         319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: R
FT   BINDING         499
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT   Optional; Condition: E
FT   BINDING         506
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT   Optional; Condition: R
XX
Size: 596-868;
Related: None;
Template: P76562; D4GW73; Q5JHC6;
Scope:
 Bacteria; Gammaproteobacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in ACTPJ, AERPE, HYPBU, IGNH4, METS5, SULAC, SULIA, SULID, SULIK,
 SULIL, SULIM, SULIN, SULIY, SULS9, SACS2, SULTO
Plasmid: None
Comments: None
XX
# Version: 17
# Last updated date: 2025-06-12
# Created date: 2010-11-04
//