Full name: tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmCD
Synonym:
GI: 218929828
Orf:
COG: COG4121
UniProt: Q8ZD36
Structures: | 3PVC | 3SGL |
Complex:
Enzyme type: methyltransferase/oxidoreductase
Position of modification - modification: t:34 - mnm5s2U
t:34 - mnm5U

Comments:

Homologue of E. coli MnmCD. In E.coli (and many other bacteria) it is a bifunctional enzyme, composed of two domains that catalyze two successive reactions at the uridine wobble position 34 in tRNA: first a deacetylation reaction of cmnm5U into nm5U, then methylation of the amine group of nm5U to form mnm5U. In other organisms they may be unlinked (separate proteins), then identified as MnmC for the deacetylase and MnmD for the methylase. In certain bacteria, the catalytic domain for the deacetylation reaction is absent in their genome and only the gene coding for MnmD is present. In other bacteria, MnmC and MnmD are both present.

Protein sequence:

MNQRPIQTATLSWNEQGTPVSEQFGDIYFSNEDGLEETHHVFLKGNGFPARFASHPQQSCIFAETGFGTG LNFLTLWRDFALFRQQSPNATLRRLHYISFEKYPLHVADLASAHARWPELASFAEQLRAQWPLPLAGCHR ILLADGAITLDLWFGDVNTLLPTLDDSLNNQVDAWFLDGFAPAKNPDMWNEQLFNAMARMTRPGGTFSTF TAAGFVRRGLQQAGFNVTKVKGFGQKREMLTGTLPQQIHAPTAPWYHRPAATRCDDIAIIGGGIVSALTA LALQRRGAVVTLYCADAQPAQGASGNRQGALYPLLNGKNDALETFFTSAFTFARRQYDQLLEQGIAFDHQ WCGVSQLAFDDKSRGKIEKMLHTQWPVEFAEAMSREQLSELAGLDCAHDGIHYPAGGWLCPSDLTHALMM LAQQNGMTCHYQHELQRLKRIDSQWQLTFGQSQAAKHHATVILATGHRLPEWEQTHHLPLSAVRGQVSHI PTTPVLSQLQQVLCYDGYLTPVNPANQHHCIGASYQRGDIATDFRLTEQQENRERLLRCLPQVSWPQQVD VSDNQARCGVRCAIRDHLPMVGAVPDYAATLAQYQDLSRRIQHGGESEVNDIAVAPVWPELFMVGGLGSR GLCSAPLVAEILAAQMFGEPLPLDAKTLAALNPNRFWIRKLLKGRPVQTRSPATQESSR

Publications:

Title Authors Journal Details PubMed Id DOI
Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC. Kim J, Almo SC BMC Struct Biol [details] 23617613 -

Links:

_PubMed_
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