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Protein

tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase

Gene

miaB

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i6A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms2i6A) at position 37 in tRNAs that read codons beginning with uridine.UniRule annotation

Catalytic activityi

N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 2-methylthio-N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi48 – 481Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi82 – 821Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi156 – 1561Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi160 – 1601Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-449-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-2-methylthio-N(6)-dimethylallyladenosine synthaseUniRule annotation (EC:2.8.4.3UniRule annotation)
Alternative name(s):
(Dimethylallyl)adenosine tRNA methylthiotransferase MiaBUniRule annotation
tRNA-i(6)A37 methylthiotransferaseUniRule annotation
Gene namesi
Name:miaBUniRule annotation
Ordered Locus Names:BUsg_426
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 439439tRNA-2-methylthio-N(6)-dimethylallyladenosine synthasePRO_0000141731Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi198804.BUsg426.

Structurei

3D structure databases

ProteinModelPortaliQ8K9C2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 119118MTTase N-terminalUniRule annotationAdd
BLAST
Domaini377 – 43963TRAMUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the methylthiotransferase family. MiaB subfamily.UniRule annotation
Contains 1 MTTase N-terminal domain.UniRule annotation
Contains 1 TRAM domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0621.
KOiK06168.
OMAiGCQMNKA.
OrthoDBiEOG6P5ZD8.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
HAMAPiMF_01864. tRNA_metthiotr_MiaB.
InterProiIPR006638. Elp3/MiaB/NifB.
IPR023970. MeThioTfrase/rSAM.
IPR005839. Methylthiotransferase.
IPR020612. Methylthiotransferase_CS.
IPR013848. Methylthiotransferase_N.
IPR006463. MiaB_methiolase.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
IPR002792. TRAM_dom.
[Graphical view]
PANTHERiPTHR11918. PTHR11918. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
PF01938. TRAM. 1 hit.
PF00919. UPF0004. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00089. TIGR00089. 1 hit.
PROSITEiPS51449. MTTASE_N. 1 hit.
PS01278. MTTASE_RADICAL. 1 hit.
PS50926. TRAM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K9C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYIYIKTWG CQMNEYDSSM ITVFLEKTGR YLITKEVEKA DILILNTCSI
60 70 80 90 100
REKAQEKVFH QLGRWKKLKN KKPDVIIAVG GCVATQEGKE IFKRANYVDI
110 120 130 140 150
VFGTQTLHKL AQMIDKVEKN RRFMIDISFP QLEKFNYSLE PKKTGYTASI
160 170 180 190 200
SIMEGCNKYC SFCVVPYTRG HEISRPSDDI LLEISILAEN GVREINLLGQ
210 220 230 240 250
NVNAYRGRTF NGKICFFSEL LRLVSEIDGI DRIRFTTSNP LEFTDDIIEV
260 270 280 290 300
YQDTPKLVSF LHLPVQSGSN RILQLMKRSY TTEEYEKIIE KLILARSNIQ
310 320 330 340 350
ISSDFIVGFP SESEEDFQKT INFIKKINFD MSFSFIYSSR PGTPASEMKD
360 370 380 390 400
NIDLQEKKKR LYTLQNCINK QTMSWSRKML KSTQSVLVEG VSKKNIMELY
410 420 430
GKTENNRIVT FKGSHKMIGK FIKLKIKKVH THSLQGELI
Length:439
Mass (Da):50,787
Last modified:October 1, 2002 - v1
Checksum:i2E83E7F58CD0E5B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67969.1.
RefSeqiNP_660758.1. NC_004061.1.
WP_011053936.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67969; AAM67969; BUsg_426.
KEGGibas:BUsg426.
PATRICi21247700. VBIBucAph100086_0450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67969.1.
RefSeqiNP_660758.1. NC_004061.1.
WP_011053936.1. NC_004061.1.

3D structure databases

ProteinModelPortaliQ8K9C2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198804.BUsg426.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM67969; AAM67969; BUsg_426.
KEGGibas:BUsg426.
PATRICi21247700. VBIBucAph100086_0450.

Phylogenomic databases

eggNOGiCOG0621.
KOiK06168.
OMAiGCQMNKA.
OrthoDBiEOG6P5ZD8.

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-449-MONOMER.

Family and domain databases

Gene3Di3.80.30.20. 1 hit.
HAMAPiMF_01864. tRNA_metthiotr_MiaB.
InterProiIPR006638. Elp3/MiaB/NifB.
IPR023970. MeThioTfrase/rSAM.
IPR005839. Methylthiotransferase.
IPR020612. Methylthiotransferase_CS.
IPR013848. Methylthiotransferase_N.
IPR006463. MiaB_methiolase.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
IPR002792. TRAM_dom.
[Graphical view]
PANTHERiPTHR11918. PTHR11918. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
PF01938. TRAM. 1 hit.
PF00919. UPF0004. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00089. TIGR00089. 1 hit.
PROSITEiPS51449. MTTASE_N. 1 hit.
PS01278. MTTASE_RADICAL. 1 hit.
PS50926. TRAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiMIAB_BUCAP
AccessioniPrimary (citable) accession number: Q8K9C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: May 27, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.