Modomics - A Database of RNA Modifications

ID Card:

Full name:	(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB
Synonym:	TM0653
GI:	15643418
COG:	COG0621
UniProt:	Q9WZC1
Alpha Fold Predicted Structure:	AF-Q9WZC1-F1
Enzyme type:	methylthiotransferase predicted
Position of modification - modification:	t:37 - ms2i6A

Protein sequence:

MRFYIKTFGCQMNENDSEAMAGLLVKEGFTPASSPEEADVVIINTCAVRRKSEEKAYSELGQVLKLKKKKKIVVGVAGCVAEKEREKFLEKGADFVLGTRAVPRVTEAVKKALEGEKVALFEDHLDEYTHELPRIRTSRHHAWVTIIHGCDRFCTYCIVPYTRGRERSRPMADILEEVKKLAEQGYREVTFLGQNVDAYGKDLKDGSSLAKLLEEASKIEGIERIWFLTSYPTDFSDELIEVIAKNPKVAKSVHLPVQSGSNRILKLMNRRYTKEEYLALLEKIRSKVPEVAISSDIIVGFPTETEEDFMETVDLVEKAQFERLNLAIYSPREGTVAWKYYKDDVPYEEKVRRMQFLMNLQKRINRKLNERYRGKTVRIIVEAQAKNGLFYGRDIRNKIIAFEGEDWMIGRFADVKVEKITAGPLYGKVVWVEKTPSPVSSSE

Comments:

Bacterial MiaB works on A36-i6A37-containing tRNA. It displays a N-terminal TRAM domain and a C-terminal catalytic radical SAM domain with two [4Fe-4S] clusters coordinated with 3 cysteines and an exchangeable S-AdoMet. Belongs to the same family of methylthiotransferases as B subtilis MtaB (YqeV), mammalian MtaB (Cdkal1) and protein methylthiotransferase RimO. A MiaB-CDKAL1-like enzyme is present in Archaea, while MiaA/Mod5 is totally absent. Its function is still elusive (2012).

Reaction	Substrate	SubstrateType	Position	(Anti)Codon	Modified (Anti)Codon	Amino Acid Change	Transcript Name	Transcript Region	Cellular Localization	References
i6A:ms2i6A	tRNA (t)	many/many/prokaryotic cytosol	37							12766153

Alpha Fold Predicted Structure:

Clear Selection and Reset Camera

Protein sequence:

M R F Y I K T F G C Q M N E N D S E A M A G L L V K E G F T P A S S P E E A D V V I I N T C A V R R K S E E K A Y S E L G Q V L K L K K K K K I V V G V A G C V A E K E R E K F L E K G A D F V L G T R A V P R V T E A V K K A L E G E K V A L F E D H L D E Y T H E L P R I R T S R H H A W V T I I H G C D R F C T Y C I V P Y T R G R E R S R P M A D I L E E V K K L A E Q G Y R E V T F L G Q N V D A Y G K D L K D G S S L A K L L E E A S K I E G I E R I W F L T S Y P T D F S D E L I E V I A K N P K V A K S V H L P V Q S G S N R I L K L M N R R Y T K E E Y L A L L E K I R S K V P E V A I S S D I I V G F P T E T E E D F M E T V D L V E K A Q F E R L N L A I Y S P R E G T V A W K Y Y K D D V P Y E E K V R R M Q F L M N L Q K R I N R K L N E R Y R G K T V R I I V E A Q A K N G L F Y G R D I R N K I I A F E G E D W M I G R F A D V K V E K I T A G P L Y G K V V W V E K T P S P V S S S E

Secondary Structure Alphabet

G: 3-turn helix (3₁₀helix)
H: α-helix
I: 𝝅-helix (5 - turn helix)
T: Hydrogen Bonded Turn
B: β-sheet
S: Bend
C: Coil (residues not present in any of the above conformations)
N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files	AF-Q9WZC1-F1.pdb
Alpha Fold Pdbx/mmCIF Files	AF-Q9WZC1-F1.cif
DSSP Secondary Structures	Q9WZC1.dssp

Publications:

Title	Authors	Journal	Details	PubMed Id	DOI
MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters.	Hernandez HL, Pierrel F, Elleingand E, Garcia-Serres R, Huynh BH, Johnson MK, Fontecave M, Atta M	Biochemistry	[details]	17407324	-
MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase.	Pierrel F, Hernandez HL, Johnson MK, Fontecave M, Atta M	J Biol Chem	[details]	12766153	-
S-Adenosylmethionine-dependent radical-based modification of biological macromolecules.	Atta M, Mulliez E, Arragain S, Forouhar F, Hunt JF, Fontecave M	Curr Opin Struct Biol	[details]	20951571	-

Links:

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