TRMB_ECOLI
ID TRMB_ECOLI Reviewed; 239 AA.
AC P0A8I5; P32049; P58089; Q2M9N3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000269|PubMed:12730187};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000303|PubMed:12730187};
GN Name=trmB; Synonyms=trmI, yggH; OrderedLocusNames=b2960, JW2927;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2001994; DOI=10.1128/jb.173.6.1902-1910.1991;
RA Tsai-Wu J.-J., Radicella J.P., Lu A.-L.;
RT "Nucleotide sequence of the Escherichia coli micA gene required for A/G-
RT specific mismatch repair: identity of micA and mutY.";
RL J. Bacteriol. 173:1902-1910(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RC STRAIN=K12 / XL1-Blue;
RX PubMed=12730187; DOI=10.1128/jb.185.10.3238-3243.2003;
RA De Bie L.G.S., Roovers M., Oudjama Y., Wattiez R., Tricot C., Stalon V.,
RA Droogmans L., Bujnicki J.M.;
RT "The yggH gene of Escherichia coli encodes a tRNA (m7G46)
RT methyltransferase.";
RL J. Bacteriol. 185:3238-3243(2003).
RN [5]
RP MUTAGENESIS OF ARG-26; ASP-144; ARG-150; HIS-151; ASN-152; ARG-154;
RP ARG-155; ASP-180; THR-217 AND GLU-220.
RX PubMed=15789416; DOI=10.1002/prot.20454;
RA Purta E., van Vliet F., Tricot C., De Bie L.G., Feder M., Skowronek K.,
RA Droogmans L., Bujnicki J.M.;
RT "Sequence-structure-function relationships of a tRNA (m7G46)
RT methyltransferase studied by homology modeling and site-directed
RT mutagenesis.";
RL Proteins 59:482-488(2005).
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057,
CC ECO:0000269|PubMed:12730187}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01057, ECO:0000269|PubMed:12730187};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01057, ECO:0000305|PubMed:12730187}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01057,
CC ECO:0000269|PubMed:12730187}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_01057,
CC ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA72956.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M59471; AAA72956.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U28377; AAA69127.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75997.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77023.1; -; Genomic_DNA.
DR PIR; G65081; G65081.
DR RefSeq; NP_417435.1; NC_000913.3.
DR RefSeq; WP_000786911.1; NZ_STEB01000001.1.
DR PDB; 3DXX; X-ray; 2.05 A; A=33-239.
DR PDB; 3DXY; X-ray; 1.50 A; A=33-239.
DR PDB; 3DXZ; X-ray; 1.58 A; A=33-239.
DR PDBsum; 3DXX; -.
DR PDBsum; 3DXY; -.
DR PDBsum; 3DXZ; -.
DR AlphaFoldDB; P0A8I5; -.
DR SMR; P0A8I5; -.
DR BioGRID; 4262358; 14.
DR DIP; DIP-36015N; -.
DR IntAct; P0A8I5; 45.
DR STRING; 511145.b2960; -.
DR jPOST; P0A8I5; -.
DR PaxDb; P0A8I5; -.
DR PRIDE; P0A8I5; -.
DR EnsemblBacteria; AAC75997; AAC75997; b2960.
DR EnsemblBacteria; BAE77023; BAE77023; BAE77023.
DR GeneID; 66673158; -.
DR GeneID; 947448; -.
DR KEGG; ecj:JW2927; -.
DR KEGG; eco:b2960; -.
DR PATRIC; fig|1411691.4.peg.3771; -.
DR EchoBASE; EB1727; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_050910_0_1_6; -.
DR InParanoid; P0A8I5; -.
DR OMA; PDPWHKS; -.
DR PhylomeDB; P0A8I5; -.
DR BioCyc; EcoCyc:EG11779-MON; -.
DR BioCyc; MetaCyc:EG11779-MON; -.
DR BRENDA; 2.1.1.33; 2026.
DR UniPathway; UPA00989; -.
DR EvolutionaryTrace; P0A8I5; -.
DR PRO; PR:P0A8I5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
DR GO; GO:0106004; P:tRNA (guanine-N7)-methylation; IMP:EcoCyc.
DR GO; GO:0030488; P:tRNA methylation; IMP:EcoCyc.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; PTHR23417; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..239
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171326"
FT REGION 150..155
FT /note="Interaction with RNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT ACT_SITE 144
FT /evidence="ECO:0000250|UniProtKB:Q12009"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 217..220
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT MUTAGEN 26
FT /note="R->A: Reduces catalytic activity over 10-fold."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 144
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 150
FT /note="R->A: Reduces catalytic activity about 3-fold."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 151
FT /note="H->A: Reduces catalytic activity over 10-fold."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 152
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 154
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 155
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 180
FT /note="D->A: Reduces catalytic activity over 10-fold."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 217
FT /note="T->A: Reduces catalytic activity over 10-fold."
FT /evidence="ECO:0000269|PubMed:15789416"
FT MUTAGEN 220
FT /note="E->A: Reduces catalytic activity 10-fold."
FT /evidence="ECO:0000269|PubMed:15789416"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:3DXY"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:3DXY"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3DXY"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:3DXY"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3DXY"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:3DXY"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3DXY"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:3DXY"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:3DXY"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:3DXY"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:3DXY"
FT STRAND 169..180
FT /evidence="ECO:0007829|PDB:3DXY"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:3DXY"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3DXY"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:3DXY"
SQ SEQUENCE 239 AA; 27307 MW; B4C8AF9A1EF85FEB CRC64;
MKNDVISPEF DENGRPLRRI RSFVRRQGRL TKGQEHALEN YWPVMGVEFS EDMLDFPALF
GREAPVTLEI GFGMGASLVA MAKDRPEQDF LGIEVHSPGV GACLASAHEE GLSNLRVMCH
DAVEVLHKMI PDNSLRMVQL FFPDPWHKAR HNKRRIVQVP FAELVKSKLQ LGGVFHMATD
WEPYAEHMLE VMSSIDGYKN LSESNDYVPR PASRPVTKFE QRGHRLGHGV WDLMFERVK
