PP_4014/Q88FR9 is the single KT2440 MnmA-family tRNA-specific
2-thiouridylase. The local record assigns EC 2.8.1.13, IPR004506, ATP-binding
features, and catalytic cysteines; the OpenScientist analysis additionally
reports conservation of the ATP-utilizing PP-loop and both catalytic cysteines.
[file:PSEPK/mnmA/mnmA-uniprot.txt "Catalyzes the 2-thiolation of uridine at the
wobble position"]
Structural work on E. coli MnmA directly establishes tRNA U34 recognition and
an adenylated RNA intermediate. PMID:16871210 ATP binding is therefore added as a missing NEW annotation from
the local UniProt record, not proposed as a new ontology term because
GO:0005524 already exists.
The relay boundary ends at MnmA-mediated sulfur incorporation. MnmE/MnmG and
MnmC-dependent side-chain elaboration are downstream and are not assigned to
MnmA. The modified wobble base has a direct decoding role, but that system-level
effect is context rather than an additional MnmA molecular function.
PMID:26791911 The full E. coli IscS-TusA-TusBCD-TusE-MnmA pathway was
reconstituted, but no direct KT2440 reconstitution was identified.
PMID:16387657