AC   MF_00144;
DC   Protein; auto
TR   HAMAP; MF_00144; -; 1; level=0
XX
Names: tRNA_thiouridyl_MnmA
XX
ID   MNMA
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA;
DE            EC=2.8.1.13;
GN   Name=mnmA;
XX
case <OC:Enterobacterales>
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC       (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation
CC       of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is
CC       provided by IscS, via a sulfur-relay system. Binds ATP and its
CC       substrate tRNAs.
CC   -!- SUBUNIT: Interacts with TusE.
else
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC       (U34) of tRNA, leading to the formation of s(2)U34.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC         tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC         cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC         Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC         ChEBI:CHEBI:456215; EC=2.8.1.13;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family.
XX
DR   Pfam; PF03054; tRNA_Me_trans; 1; trigger=no
DR   NCBIfam; TIGR00420; TrmU; 1; trigger=no
XX
KW   ATP-binding
KW   Cytoplasm
KW   Nucleotide-binding
KW   RNA-binding
KW   Transferase
KW   tRNA processing
KW   tRNA-binding
XX
GO   GO:0016740; F:transferase activity
GO   GO:0006400; P:tRNA modification
GO   GO:0005737; C:cytoplasm
case <FTTag:disulf>
KW   Disulfide bond
end case
XX
FT   From: MNMA_ECOLI (P25745)
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [GAL]-x-S-G-x-x-[DE]-S
FT   REGION          97..99
FT                   /note="Interaction with target base in tRNA"
FT   Optional; Condition: N-P-D
FT   REGION          149..151
FT                   /note="Interaction with tRNA"
FT   Optional; Condition: [KR]-[DEN]-Q
FT   REGION          311..312
FT                   /note="Interaction with tRNA"
FT   Optional; Condition: [RK]-Y
FT   ACT_SITE        102
FT                   /note="Nucleophile"
FT   Condition: C
FT   ACT_SITE        199
FT                   /note="Cysteine persulfide intermediate"
FT   Condition: C
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: [MLFI]
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: G
FT   SITE            128
FT                   /note="Interaction with tRNA"
FT   Optional; Condition: H
FT   SITE            344
FT                   /note="Interaction with tRNA"
FT   Optional; Condition: Q
FT   DISULFID        102..199
FT                   /note="Alternate"
FT   Tag: disulf; Condition: C-x*-C
XX
Size: 338-431;
Related: None;
Template: P25745; Q97T38;
Scope:
 Bacteria
Fusion:
 Nter: <nifU>; <ribF>
 Cter: None
Duplicate: in ALIB4, BACFN, BACFR, BACTN, PHOV8, CLOB1, CLOBH, CLOBK, CLOBL,
 CLOBM, CLOTE, FUSNN, GEOKA, SYNAS, THEP3, THEPX, CALS4, XANOP
Plasmid: None
Comments: Shorter N-terminus in THEM4 and in the second copy of SYNAS; sequences
 not included in alignment and not taken into account in size range.
XX
# Revision 1.36 2023/06/01
//