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Protein

tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ

Gene

trmJ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA (PubMed:16848900, PubMed:24951554, PubMed:26202969). Can also methylate adenosine or guanosine, even though these nucleosides are rare or absent at position 32 in the anticodon loop of tRNA (PubMed:24951554).3 Publications

Catalytic activityi

S-adenosyl-L-methionine + cytidine(32) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(32) in tRNA.3 Publications
S-adenosyl-L-methionine + uridine(32) in tRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(32) in tRNA.3 Publications

Kineticsi

kcat is 1.52 min(-1) with tRNA(fMet1) as substrate. kcat is 1.42 min(-1) with tRNA(fMet2) as substrate. kcat is 1.31 min(-1) with tRNA(Trp1) as substrate. kcat is 1.20 min(-1) with tRNA(Gln1) as substrate. kcat is 1.41 min(-1) with tRNA(Gln2) as substrate. kcat is 2.30 min(-1) with tRNA(Ser1) as substrate.1 Publication
  1. KM=0.67 µM for tRNA(fMet1)1 Publication
  2. KM=0.81 µM for tRNA(fMet2)1 Publication
  3. KM=0.94 µM for tRNA(Trp1)1 Publication
  4. KM=9.88 µM for tRNA(Gln1)1 Publication
  5. KM=5.79 µM for tRNA(Gln2)1 Publication
  6. KM=11.82 µM for tRNA(Ser1)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei114S-adenosyl-L-methionine; via amide nitrogen2 Publications1
    Binding sitei134S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen2 Publications1

    GO - Molecular functioni

    • RNA binding Source: InterPro
    • tRNA (cytosine-2'-O-)-methyltransferase activity Source: EcoCyc
    • tRNA (uracil-2'-O-)-methyltransferase activity Source: EcoCyc

    GO - Biological processi

    • tRNA nucleoside ribose methylation Source: EcoCyc

    Keywordsi

    Molecular functionMethyltransferase, Transferase
    Biological processtRNA processing
    LigandS-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciEcoCyc:G7327-MONOMER
    MetaCyc:G7327-MONOMER
    BRENDAi2.1.1.200 2026

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJCurated (EC:2.1.1.2003 Publications)
    Alternative name(s):
    TrMet(Xm32)1 Publication
    tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferaseCurated
    tRNA Cm32/Um32 methyltransferaseCurated
    Gene namesi
    Name:trmJ1 Publication
    Synonyms:yfhQ
    Ordered Locus Names:b2532, JW2516
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13452 trmJ

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi23R → A: Loss of activity. 1 Publication1
    Mutagenesisi82R → A: Loss of tRNA binding affinity. Loss of activity. 1 Publication1
    Mutagenesisi84R → A: Loss of tRNA binding affinity. Loss of activity. 1 Publication1
    Mutagenesisi115R → A: No change in tRNA binding affinity. No change in activity. 1 Publication1
    Mutagenesisi140Y → F: Strong decrease in activity. 1 Publication1
    Mutagenesisi172H → A: No change in activity. 1 Publication1
    Mutagenesisi175T → A: No change in activity. 1 Publication1
    Mutagenesisi177Y → A: No change in activity. 1 Publication1
    Mutagenesisi199F → A: Strong decrease in activity. 1 Publication1
    Mutagenesisi211K → A: Strong decrease in tRNA binding affinity. Strong decrease in activity. 1 Publication1
    Mutagenesisi213R → A: Strong decrease in tRNA binding affinity. Loss of activity. 1 Publication1
    Mutagenesisi214R → A: Strong decrease in tRNA binding affinity. Strong decrease in activity. 1 Publication1
    Mutagenesisi218R → A: Strong decrease in tRNA binding affinity. Strong decrease in activity. 1 Publication1
    Mutagenesisi225E → A: Loss of activity. 1 Publication1
    Mutagenesisi228I → A: Strong decrease in activity. 1 Publication1
    Mutagenesisi229L → A: Loss of activity. 1 Publication1
    Mutagenesisi231G → A: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001598241 – 246tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJAdd BLAST246

    Proteomic databases

    PaxDbiP0AE01
    PRIDEiP0AE01

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi4263050, 19 interactors
    IntActiP0AE01, 3 interactors
    STRINGi316385.ECDH10B_2699

    Structurei

    Secondary structure

    1246
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi2 – 4Combined sources3
    Beta strandi5 – 11Combined sources7
    Helixi15 – 27Combined sources13
    Beta strandi32 – 37Combined sources6
    Helixi44 – 50Combined sources7
    Helixi51 – 53Combined sources3
    Helixi54 – 58Combined sources5
    Beta strandi61 – 64Combined sources4
    Helixi66 – 70Combined sources5
    Beta strandi74 – 79Combined sources6
    Beta strandi84 – 86Combined sources3
    Helixi93 – 104Combined sources12
    Beta strandi109 – 113Combined sources5
    Turni116 – 118Combined sources3
    Helixi122 – 125Combined sources4
    Beta strandi129 – 132Combined sources4
    Helixi145 – 162Combined sources18
    Helixi180 – 196Combined sources17
    Helixi207 – 218Combined sources12
    Helixi223 – 237Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4CNDX-ray1.50A/B1-246[»]
    4CNEX-ray1.90A/B1-246[»]
    4XBOX-ray2.60A/B1-246[»]
    ProteinModelPortaliP0AE01
    SMRiP0AE01
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni79 – 81S-adenosyl-L-methionine binding2 Publications3
    Regioni141 – 143S-adenosyl-L-methionine binding2 Publications3

    Domaini

    Both the catalytic N-terminal domain and the extensional C-terminal domain play key roles in tRNA binding and methylation.1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105CVS Bacteria
    COG0565 LUCA
    HOGENOMiHOG000229628
    InParanoidiP0AE01
    KOiK15396
    OMAiPIMNLSH
    PhylomeDBiP0AE01

    Family and domain databases

    Gene3Di3.40.1280.10, 1 hit
    InterProiView protein in InterPro
    IPR029028 Alpha/beta_knot_MTases
    IPR004384 rRNA_MeTrfase_TrmH_1
    IPR001537 SpoU_MeTrfase
    IPR029026 tRNA_m1G_MTases_N
    PANTHERiPTHR42786 PTHR42786, 1 hit
    PfamiView protein in Pfam
    PF00588 SpoU_methylase, 1 hit
    PIRSFiPIRSF004808 LasT, 1 hit
    SUPFAMiSSF75217 SSF75217, 1 hit
    TIGRFAMsiTIGR00050 rRNA_methyl_1, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P0AE01-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLQNIRIVLV ETSHTGNMGS VARAMKTMGL TNLWLVNPLV KPDSQAIALA
    60 70 80 90 100
    AGASDVIGNA HIVDTLDEAL AGCSLVVGTS ARSRTLPWPM LDPRECGLKS
    110 120 130 140 150
    VAEAANTPVA LVFGRERVGL TNEELQKCHY HVAIAANPEY SSLNLAMAVQ
    160 170 180 190 200
    VIAYEVRMAW LATQENGEQV EHEETPYPLV DDLERFYGHL EQTLLATGFI
    210 220 230 240
    RENHPGQVMN KLRRLFTRAR PESQELNILR GILASIEQQN KGNKAE
    Length:246
    Mass (Da):27,048
    Last modified:December 6, 2005 - v1
    Checksum:i83C1AE4507E097D2
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC75585.1
    AP009048 Genomic DNA Translation: BAA16426.1
    PIRiC65030
    RefSeqiNP_417027.1, NC_000913.3
    WP_000940019.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC75585; AAC75585; b2532
    BAA16426; BAA16426; BAA16426
    GeneIDi948610
    KEGGiecj:JW2516
    eco:b2532
    PATRICifig|511145.12.peg.2633

    Similar proteinsi

    Entry informationi

    Entry nameiTRMJ_ECOLI
    AccessioniPrimary (citable) accession number: P0AE01
    Secondary accession number(s): P76993, P77438
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: April 25, 2018
    This is version 96 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health