MIAB_MYCA1
ID MIAB_MYCA1 Reviewed; 715 AA.
AC A0QIR4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase;
DE EC=2.8.4.3;
DE AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB;
DE AltName: Full=tRNA-i(6)A37 methylthiotransferase;
GN Name=miaB; OrderedLocusNames=MAV_3625;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine
CC (i(6)A), leading to the formation of 2-methylthio-N6-
CC (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read
CC codons beginning with uridine. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in
CC tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-
CC dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur
CC carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:37067, Rhea:RHEA-COMP:10375, Rhea:RHEA-COMP:10376,
CC Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29917, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64428, ChEBI:CHEBI:74415,
CC ChEBI:CHEBI:74417; EC=2.8.4.3;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC methylthiotransferase family. MiaB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK67615.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000479; ABK67615.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0QIR4; -.
DR SMR; A0QIR4; -.
DR EnsemblBacteria; ABK67615; ABK67615; MAV_3625.
DR KEGG; mav:MAV_3625; -.
DR HOGENOM; CLU_399980_0_0_11; -.
DR Proteomes; UP000001574; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.12160; -; 1.
DR Gene3D; 3.80.30.20; -; 1.
DR HAMAP; MF_01864; tRNA_metthiotr_MiaB; 1.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR006463; MiaB_methiolase.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR InterPro; IPR002792; TRAM_dom.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDF00273; (dimethylallyl)adenosine_tRNA; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00089; TIGR00089; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
DR PROSITE; PS50926; TRAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW S-adenosyl-L-methionine; Transferase; Transmembrane; Transmembrane helix;
KW tRNA processing.
FT CHAIN 1..715
FT /note="tRNA-2-methylthio-N(6)-dimethylallyladenosine
FT synthase"
FT /id="PRO_0000374665"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 29..146
FT /note="MTTase N-terminal"
FT DOMAIN 169..405
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 408..475
FT /note="TRAM"
FT REGION 1..516
FT /note="(Dimethylallyl)adenosine tRNA methylthiotransferase
FT MiaB"
FT REGION 517..715
FT /note="Unknown"
FT BINDING 38
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 77192 MW; 9CE567BF32FBC8C9 CRC64;
MTCGFSRADR SPYHGPVTST VARDVSGVRT YQVRTYGCQM NVHDSERLAG LLEAAGYRRA
AEGAEVADVV VFNTCAVREN ADNKLYGNLS HLAPRKRSNP QMQIAVGGCL AQKDREAVLR
RAPWVDVVFG THNIGSLPTL LERARHNKAA QVEIAEALQQ FPSSLPSARE SAYAAWVSIS
VGCNNSCTFC IVPSLRGKEV DRSPDDILAE VRSLVADGVL EVTLLGQNVN AYGVSFADPA
LPRDRGAFAR LLRACGEIDG LERVRFTSPH PAEFTDDVIE AMAQTPNVCP ALHMPLQSGS
DRVLRAMRRS YRAERYLGII DRVRAAMPHA AITTDLIVGF PGETEEDFAA TLDVVRRARF
AAAFTFQYSK RPGTPAAELD GQIPKAVVQE RYERLVELQE SISLQGNQAL VGQTVELLVA
TGEGRKDSAT ARMSGRARDG RLVHFAADDR VRPGDLVTTV ITGAAPHHLI ADAGILSHRR
TRAGDAHAPA GARAASVSAC PPSGRRRPGP TRWMCLMNDD RNHDDPRLGA LRTEIEAAER
RVAGGIDPGA RGFVVSILVF VLLGSFILPH TGDVRGWDVL FGTHDAGAAA VALPSRVFGW
LALVFGVGFS TLALVTRRWA LAWIALAGTA IAGAAGMLAI WSRQTVPAGH PGPGWGLIVA
WITVLVLIYQ WARVVWSRTI VQLAAEEQRR RVAAQQQSTT LLDDLPKPED PAAGT
