MIAE_SALTY
ID MIAE_SALTY Reviewed; 270 AA.
AC Q08015;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=tRNA 2-(methylsulfanyl)-N(6)-isopentenyladenosine(37) hydroxylase {ECO:0000305};
DE EC=1.14.99.69 {ECO:0000269|PubMed:17679698, ECO:0000269|PubMed:23906247, ECO:0000269|PubMed:8253666};
DE AltName: Full=2-methylthio-N6-isopentenyladenosine(37)-tRNA monooxygenase {ECO:0000303|PubMed:23906247};
DE AltName: Full=tRNA-(ms[2]io[6]A37)-hydroxylase {ECO:0000303|PubMed:8253666};
GN Name=miaE {ECO:0000303|PubMed:8253666}; OrderedLocusNames=STM4471;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=LT2;
RX PubMed=8253666; DOI=10.1128/jb.175.24.7776-7785.1993;
RA Persson B.C., Bjoerk G.R.;
RT "Isolation of the gene (miaE) encoding the hydroxylase involved in the
RT synthesis of 2-methylthio-cis-ribozeatin in tRNA of Salmonella typhimurium
RT and characterization of mutants.";
RL J. Bacteriol. 175:7776-7785(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9620964; DOI=10.1128/jb.180.12.3144-3151.1998;
RA Persson B.C., Olafsson O., Lundgren H.K., Hederstedt L., Bjoerk G.R.;
RT "The ms2io6A37 modification of tRNA in Salmonella typhimurium regulates
RT growth on citric acid cycle intermediates.";
RL J. Bacteriol. 180:3144-3151(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBUNIT.
RX PubMed=17679698; DOI=10.1073/pnas.0704338104;
RA Mathevon C., Pierrel F., Oddou J.L., Garcia-Serres R., Blondin G.,
RA Latour J.M., Menage S., Gambarelli S., Fontecave M., Atta M.;
RT "tRNA-modifying MiaE protein from Salmonella typhimurium is a nonheme
RT diiron monooxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13295-13300(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=23906247; DOI=10.1021/bi4000832;
RA Corder A.L., Subedi B.P., Zhang S., Dark A.M., Foss F.W. Jr., Pierce B.S.;
RT "Peroxide-shunt substrate-specificity for the Salmonella typhimurium O2-
RT dependent tRNA modifying monooxygenase (MiaE).";
RL Biochemistry 52:6182-6196(2013).
RN [6]
RP FUNCTION, COFACTOR, AND DOMAIN.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=25453905; DOI=10.1021/bi5012207;
RA Subedi B.P., Corder A.L., Zhang S., Foss F.W. Jr., Pierce B.S.;
RT "Steady-state kinetics and spectroscopic characterization of enzyme-tRNA
RT interactions for the non-heme diiron tRNA-monooxygenase, MiaE.";
RL Biochemistry 54:363-376(2015).
CC -!- FUNCTION: Involved in specific tRNA modification. Catalyzes the oxygen-
CC dependent hydroxylation of 2-methylthio-N-6-isopentenyl adenosine
CC (ms2i6A) to produce 2-methylthio-N-6-(cis-hydroxy)isopentenyl adenosine
CC (ms2io6A) at position 37 in tRNAs (PubMed:8253666, PubMed:17679698,
CC PubMed:23906247). Can also use N6-(dimethylallyl)adenosine (i6A) as
CC substrate, with lower efficiency (PubMed:23906247, PubMed:25453905).
CC The presence of the hydroxyl group on the tRNA may regulate the ability
CC of S.typhimurium to grow on the citric acid cycle (CAC) intermediates
CC succinate, fumarate and malate (PubMed:9620964).
CC {ECO:0000269|PubMed:17679698, ECO:0000269|PubMed:23906247,
CC ECO:0000269|PubMed:25453905, ECO:0000269|PubMed:8253666,
CC ECO:0000269|PubMed:9620964}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + AH2
CC + O2 = A + H2O + N(6)-[(2E)-4-hydroxy-3-methylbut-2-en-1-yl]-2-
CC (methylsulfanyl)adenosine(37) in tRNA; Xref=Rhea:RHEA:65812,
CC Rhea:RHEA-COMP:10376, Rhea:RHEA-COMP:17048, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:74417, ChEBI:CHEBI:157739; EC=1.14.99.69;
CC Evidence={ECO:0000269|PubMed:17679698, ECO:0000269|PubMed:23906247,
CC ECO:0000269|PubMed:8253666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65813;
CC Evidence={ECO:0000269|PubMed:17679698, ECO:0000269|PubMed:23906247,
CC ECO:0000269|PubMed:8253666};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:17679698, ECO:0000269|PubMed:23906247,
CC ECO:0000269|PubMed:25453905};
CC Note=Contains a nonheme dinuclear iron cluster (PubMed:17679698,
CC PubMed:23906247, PubMed:25453905). Contains three different forms of
CC the dinuclear site: an hydroxo-bridged FeIII-OH-FeIII center, an oxo-
CC bridged FeIII-O-FeIII center and an hydroxo-bridged FeII-OH-FeIII
CC mixed-valent center (PubMed:17679698). {ECO:0000269|PubMed:17679698,
CC ECO:0000269|PubMed:23906247, ECO:0000269|PubMed:25453905};
CC -!- PATHWAY: tRNA modification; 2-methylthio-N-6-(cis-hydroxy)isopentenyl
CC adenosine-tRNA biosynthesis. {ECO:0000269|PubMed:17679698,
CC ECO:0000269|PubMed:8253666}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17679698,
CC ECO:0000269|PubMed:23906247}.
CC -!- DOMAIN: Binding of tRNA to MiaE induces a protein conformational change
CC that influences the electronic structure of the diiron site.
CC {ECO:0000269|PubMed:25453905}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant shows normal growth
CC characteristics after being shifted from anaerobic to aerobic
CC conditions (PubMed:8253666). Mutant shows slower growth on citrate and
CC acetate, and is unable to grow on the citric acid cycle intermediates
CC succinate, fumarate and malate (PubMed:8253666, PubMed:9620964).
CC {ECO:0000269|PubMed:8253666, ECO:0000269|PubMed:9620964}.
CC -!- SIMILARITY: Belongs to the MiaE family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X73368; CAA51782.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23290.1; -; Genomic_DNA.
DR PIR; S34361; S34361.
DR RefSeq; NP_463331.1; NC_003197.2.
DR RefSeq; WP_000218459.1; NC_003197.2.
DR AlphaFoldDB; Q08015; -.
DR SMR; Q08015; -.
DR STRING; 99287.STM4471; -.
DR PaxDb; Q08015; -.
DR EnsemblBacteria; AAL23290; AAL23290; STM4471.
DR GeneID; 1255997; -.
DR KEGG; stm:STM4471; -.
DR PATRIC; fig|99287.12.peg.4706; -.
DR HOGENOM; CLU_056571_0_0_6; -.
DR OMA; CEFKAAS; -.
DR PhylomeDB; Q08015; -.
DR BioCyc; MetaCyc:STM4471-MON; -.
DR BioCyc; SENT99287:STM4471-MON; -.
DR BRENDA; 1.14.99.69; 5542.
DR UniPathway; UPA00729; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0045301; F:tRNA-(2-methylthio-N-6-(cis-hydroxy)isopentenyl adenosine)-hydroxylase activity; IEA:InterPro.
DR CDD; cd07910; MiaE; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR010386; tRNA-Hydrxlase_MiaE.
DR PANTHER; PTHR42637; PTHR42637; 1.
DR Pfam; PF06175; MiaE; 1.
DR PIRSF; PIRSF020736; MiaE; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW tRNA processing.
FT CHAIN 1..270
FT /note="tRNA 2-(methylsulfanyl)-N(6)-
FT isopentenyladenosine(37) hydroxylase"
FT /id="PRO_0000096480"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q88KV1"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q88KV1"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q88KV1"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q88KV1"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q88KV1"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q88KV1"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q88KV1"
SQ SEQUENCE 270 AA; 31140 MW; 40CDEBEED149033C CRC64;
MTVRQRLLSY FFNRLRMNYP QILSPVLNFL HCPTPQAWIV QARDPQNLPL LLTDHLICEL
KAAQTALLLV RKYVADKSGA DALLSWLQPY EAFAFRQGPE PDFVALHKQI SKSAMPQTDD
PWGRQLIDRM VLLIKEELHH FWQVREVMQA RNIPYVKITA SRYAKGMLKA VRTHEPLTLI
DKLICGAYIE ARSCERFAAL APWLDEDLQT FYLSLLRSEA RHYQDYLALA QQISAEDISA
RVRYFGEVEA DLILSPDREF RFHSGVPAAG
