Full name: MnmD tRNA methyltransferase
Synonym: MnmC2
GI: 15606976
Orf: aq_1980
COG: COG752
UniProt: O67789
Structures: | 3VYW |
Complex:
Enzyme type: methyltransferase
Position of modification - modification: t:34 - mnm5s2U
t:34 - mnm5U

Comments:

In E.coli (and many other bacteria) MnmCD 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:

MKREEYLKNYLESYLRKKEVSLTEEEFNVILREFLRFAYNPEESGQEIADTADGSKTLIHKTYGEPYHSQ TAGAIRESLYKFVRPSRILEKAKERKVIRILDVGFGLGYNLAVALKHLWEVNPKLRVEIISFEKELLKEF PILPEPYREIHEFLLERVPEYEGERLSLKVLLGDARKRIKEVENFKADAVFHDAFSPYKNPELWTLDFLS LIKERIDEKGYWVSYSSSLSVRKSLLTLGFKVGSSREIGRKRKGTVASLKAPVPPMEENEVRKLVLSPFA VPMRDEKLDKEPLEILIDYLLKVYKISR

Enzymatic activities:

Reaction Substrate Type Position
nm5U:mnm5U tRNA (t) 34
nm5s2U:mnm5s2U tRNA (t) 34

Publications:

Title Authors Journal Details PubMed Id DOI
Characterization and structure of the Aquifex aeolicus protein DUF752: a bacterial tRNA-methyltransferase (MnmC2) functioning without the usually fused oxidase domain (MnmC1). Kitamura A, Nishimoto M, Sengoku T, Shibata R, Jager G, Bjork GR, Grosjean H, Yokoyama S, Bessho Y... J Biol Chem [details] 23091054 -

Links:

_PubMed_
Copyright © Genesilico - All rights reserved
If you have any advice or suggestions for corrections or improvements, please contact: Pietro Boccaletto