AC MF_01849; DC Protein; auto TR HAMAP; MF_01849; -; 1; level=0 XX Names: RNA_methyltr_RlmN XX ID RLMN case DE RecName: Full=Dual-specificity RNA methyltransferase RlmN; DE EC=2.1.1.192; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase; DE AltName: Full=23S rRNA m2A2503 methyltransferase; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase; DE AltName: Full=tRNA m2A37 methyltransferase; else case DE RecName: Full=Probable dual-specificity RNA methyltransferase RlmN; DE EC=2.1.1.192; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase; DE AltName: Full=23S rRNA m2A2503 methyltransferase; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase; DE AltName: Full=tRNA m2A37 methyltransferase; else DE RecName: Full=Ribosomal RNA large subunit methyltransferase N; DE EC=2.1.1.-; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase; DE AltName: Full=23S rRNA m2A2503 methyltransferase; end case GN Name=rlmN; XX case CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S CC rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems CC to play a crucial role in the proofreading step occurring at the CC peptidyl transferase center and thus would serve to optimize ribosomal CC fidelity. else case CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S CC rRNA and position 2 of adenine 37 in tRNAs. Confers resistance to some CC classes of antibiotics. else case CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S CC rRNA and position 2 of adenine 37 in tRNAs. end case case CC -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S CC rRNA. end case case CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] CC + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + CC 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA- CC COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; EC=2.1.1.192; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S- CC adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'- CC deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S- CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:43332, Rhea:RHEA-COMP:10000, CC Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10485, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; EC=2.1.1.192; end case case CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] CC + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + CC 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA- CC COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74497; EC=2.1.1.192; end case case CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine.; end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving CC intermediate methylation of a conserved cysteine residue. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. XX DR Pfam; PF04055; Radical_SAM; 1; trigger=no DR NCBIfam; TIGR00048; TIGR00048; 1; trigger=no DR PIRSF; PIRSF006004; CHP00048; 1; trigger=no DR PROSITE; PS51918; RADICAL_SAM; 1; trigger=yes XX KW Cytoplasm KW Disulfide bond KW Methyltransferase KW rRNA processing KW S-adenosyl-L-methionine KW Transferase case KW 4Fe-4S KW Iron KW Iron-sulfur KW Metal-binding end case case KW Antibiotic resistance end case case KW tRNA processing end case XX GO GO:0019843; F:rRNA binding GO GO:0070040; F:rRNA (adenine(2503)-C2-)-methyltransferase activity GO GO:0070475; P:rRNA base methylation case GO GO:0000049; F:tRNA binding GO GO:0002935; F:tRNA (adenine(37)-C2)-methyltransferase activity GO GO:0030488; P:tRNA methylation end case case GO GO:0051539; F:4 iron, 4 sulfur cluster binding end case GO GO:0005737; C:cytoplasm XX FT From: RLMN_ECOLI (P36979) FT BINDING 179..180 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G-E FT BINDING 233..235 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S-x-[HNT] FT ACT_SITE 105 FT /note="Proton acceptor" FT Condition: E FT ACT_SITE 355 FT /note="S-methylcysteine intermediate" FT Condition: C FT BINDING 125 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Group: 1; Condition: C FT BINDING 129 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Group: 1; Condition: C FT BINDING 132 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Group: 1; Condition: C FT BINDING 211 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S FT BINDING 312 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [NTH] FT DISULFID 118..355 FT /note="(transient)" FT Condition: C-x*-C XX Size: 318-431; Related: MF_01873; Template: P36979; A6QGB8; Scope: Bacteria Archaea Fusion: Nter: None Cter: None Duplicate: in MYXXD, OPITP, PARUW, XANOP Plasmid: None Comments: Possible wrong starts. XX # Revision 1.22 2023/10/13 //