| 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:
MKREEYLKNYLESYLRKKEVSLTEEEFNVILREFLRFAYNPEESGQEIADTADGSKTLIHKTYGEPYHSQTAGAIRESLYKFVRPSRILEKAKERKVIRI
LDVGFGLGYNLAVALKHLWEVNPKLRVEIISFEKELLKEFPILPEPYREIHEFLLERVPEYEGERLSLKVLLGDARKRIKEVENFKADAVFHDAFSPYKN
PELWTLDFLSLIKERIDEKGYWVSYSSSLSVRKSLLTLGFKVGSSREIGRKRKGTVASLKAPVPPMEENEVRKLVLSPFAVPMRDEKLDKEPLEILIDYL
LKVYKISR
Enzymatic activities:
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:
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