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MIAB_PROM5
ID   MIAB_PROM5              Reviewed;         464 AA.
AC   A2BY12;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=tRNA-2-methylthio-N(6)-dimethylallyladenosine synthase {ECO:0000255|HAMAP-Rule:MF_01864};
DE            EC=2.8.4.3 {ECO:0000255|HAMAP-Rule:MF_01864};
DE   AltName: Full=(Dimethylallyl)adenosine tRNA methylthiotransferase MiaB {ECO:0000255|HAMAP-Rule:MF_01864};
DE   AltName: Full=tRNA-i(6)A37 methylthiotransferase {ECO:0000255|HAMAP-Rule:MF_01864};
GN   Name=miaB {ECO:0000255|HAMAP-Rule:MF_01864}; OrderedLocusNames=P9515_14661;
OS   Prochlorococcus marinus (strain MIT 9515).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9515;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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:0000255|HAMAP-Rule:MF_01864}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01864};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01864};
CC       Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_01864};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01864}.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. MiaB
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01864}.
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DR   EMBL; CP000552; ABM72673.1; -; Genomic_DNA.
DR   RefSeq; WP_011820770.1; NC_008817.1.
DR   AlphaFoldDB; A2BY12; -.
DR   SMR; A2BY12; -.
DR   STRING; 167542.P9515_14661; -.
DR   PRIDE; A2BY12; -.
DR   EnsemblBacteria; ABM72673; ABM72673; P9515_14661.
DR   KEGG; pmc:P9515_14661; -.
DR   eggNOG; COG0621; Bacteria.
DR   HOGENOM; CLU_018697_2_2_3; -.
DR   OMA; CEHFHIP; -.
DR   OrthoDB; 397139at2; -.
DR   Proteomes; UP000001589; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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; PF01938; TRAM; 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; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..464
FT                   /note="tRNA-2-methylthio-N(6)-dimethylallyladenosine
FT                   synthase"
FT                   /id="PRO_0000374451"
FT   DOMAIN          19..135
FT                   /note="MTTase N-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT   DOMAIN          156..393
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   DOMAIN          396..464
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT   BINDING         28
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT   BINDING         64
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT   BINDING         98
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01864"
FT   BINDING         170
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:0000255|HAMAP-Rule:MF_01864"
FT   BINDING         174
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:0000255|HAMAP-Rule:MF_01864"
FT   BINDING         177
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:0000255|HAMAP-Rule:MF_01864"
SQ   SEQUENCE   464 AA;  53153 MW;  9F3034E40D4B6F71 CRC64;
     MLTKTIQEEK KTPKDESIGS YWITTFGCQM NKADSERMAG TLEKMGYSRA IDELKADLVL
     YNTCTIRDSA QQKVYSFLGR QIKRKHSLPK LKLVVAGCLA QQEGESLLRR VPELDLIMGP
     QHVNNLENLL ERVDSGNQVV ATEETFISED ITNARRDSTI CGWVNIIYGC NERCSYCVVP
     SVRGKEQSRY PKAIKSEIQT LAQNNYKEIT LLGQNIDAYG RDLPVTTKEG RKENTLTDLL
     YFIHDVDGIR RIRFSTSHPK YFSKRLIKAC YELDKVCEHF HIPFQSGNDE ILRLMARGYT
     IDKYKKIIEN IRSLMPNASI TADAIVAFPG ETEKQYQDTL RLISDVGFDQ VMTAAYSPRP
     NTPAAIWNNQ IAEEVKKERL KEINELVEAT SRKRNQRYLN NTESVLIEGL NPKNSMQMMG
     RTRTNRLTFV EIPENIEFNY SFGDELNVKI TEARSFSLSG QIYK
 
 
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