ID   2.3.1.311
DE   tRNA carboxymethyluridine synthase.
CA   acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in tRNA =
CA   5'-deoxyadenosine + 5-(carboxymethyl)uridine(34) in tRNA + CoA + 2 H(+) +
CA   L-methionine.
CC   -!- The enzyme, found in eukaryotes, most archaea, and some bacteria,
CC       catalyzes the first step in modification of the wobble uridine base
CC       of certain tRNAs.
CC   -!- In eukaryotes the enzyme is a complex of six conserved subunits, with
CC       ELP3 being the catalytic subunit.
CC   -!- In archaea and bacteria the enzyme consists of a single subunit,
CC       homologous to ELP3.
CC   -!- The enzyme contains an [4Fe-4S] cluster and uses radical chemistry. A
CC       5'-deoxyadenosyl radical generated in the radical AdoMet (SAM) domain
CC       attacks the acetyl-CoA donor, activating its methyl group, which
CC       forms a C-C bond with C5 of the uridine moiety.
DR   Q93ZR1, ELP3_ARATH ;  Q2KJ61, ELP3_BOVIN ;  Q60LW7, ELP3_CAEBR ;
DR   Q23651, ELP3_CAEEL ;  Q5ZHS1, ELP3_CHICK ;  Q5RIC0, ELP3_DANRE ;
DR   A0A1C7D1B7, ELP3_DEHMC ;  Q1ZXC6, ELP3_DICDI ;  Q9VQZ6, ELP3_DROME ;
DR   Q9H9T3, ELP3_HUMAN ;  D5VRB9, ELP3_METIM ;  Q58536, ELP3_METJA ;
DR   Q9CZX0, ELP3_MOUSE ;  Q7X7L3, ELP3_ORYSJ ;  O14023, ELP3_SCHPO ;
DR   Q5HZM6, ELP3_XENLA ;  Q6NVL5, ELP3_XENTR ;  Q02908, ELP3_YEAST ;
//