Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup methylthiotransferase

     ⌊ Family (dimethylallyl)adenosine tRNA methylthiotransferase (MiaB-like)

  ⌊ FunctionalDomain (Dimethylallyl)adenosine tRNA methylthiotransferase (ID 380381)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM IES PubMed:12766153 PubMed:15339930 PubMed:17407324
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermotoga maritima MSB8 Taxon ID: 243274 15643418 NP_228462.1 (RefSeq) PRP URP
Thermotoga maritima Taxon ID: 2336 490182526 WP_004081141.1 (RefSeq) URP
Thermotoga maritima Taxon ID: 2336 811641903 AKE30312.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000255|HAMAP-Rule:MF_01864} Q9WZC1 MIAB_THEMA (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 443 | Length of Functional Domain: 435

1       10        20        30        40        50        60

MRFYIKTFGCQMNENDSEAMAGLLVKEGFTPASSPEEADVVIINTCAVRRKSEEKAYSEL
GQVLKLKKKKKIVVGVAGCVAEKEREKFLEKGADFVLGTRAVPRVTEAVKKALEGEKVAL
FEDHLDEYTHELPRIRTSRHHAWVTIIHGCDRFCTYCIVPYTRGRERSRPMADILEEVKK
LAEQGYREVTFLGQNVDAYGKDLKDGSSLAKLLEEASKIEGIERIWFLTSYPTDFSDELI
EVIAKNPKVAKSVHLPVQSGSNRILKLMNRRYTKEEYLALLEKIRSKVPEVAISSDIIVG
FPTETEEDFMETVDLVEKAQFERLNLAIYSPREGTVAWKYYKDDVPYEEKVRRMQFLMNL
QKRINRKLNERYRGKTVRIIVEAQAKNGLFYGRDIRNKIIAFEGEDWMIGRFADVKVEKI
TAGPLYGKVVWVEKTPSPVSSSE
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
150 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
154 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
157 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 3/3 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
150 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
154 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
157 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
10 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
46 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
79 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
150 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
154 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
157 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS

Catalyzed Reaction

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

+ + 2 + + + + + + + 2
thiol group
29917		 N(6)-dimethylallyladenine 5'-monophosphate(1-) residue
74415		 S-adenosyl-L-methionine zwitterion
59789		 hydrogen donor
17499		 H group
64428		 2-methylthio-N(6)-dimethylallyladenine 5'-monophosphate(1-) residue
74417		 5'-deoxyadenosine
17319		 S-adenosyl-L-homocysteine zwitterion
57856		 L-methionine zwitterion
57844		 hydrogen acceptor
13193		 hydron
15378

EC: 2.8.4.3 | IntEnz: 2.8.4.3 | Kegg: 2.8.4.3 | BioCyc: 2.8.4.3 | BRENDA: 2.8.4.3

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:29 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 443 442
July 15, 2014, 5:16 a.m. update domain end position 442 435
EC number assigned by UniProtKB accession ID.