ID A0A293TT00_HELPX Unreviewed; 357 AA. AC A0A293TT00; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 07-OCT-2020, entry version 13. DE RecName: Full=Dual-specificity RNA methyltransferase RlmN {ECO:0000256|HAMAP-Rule:MF_01849}; DE EC=2.1.1.192 {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; DE AltName: Full=tRNA m2A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849}; GN Name=rlmN {ECO:0000256|HAMAP-Rule:MF_01849, GN ECO:0000313|EMBL:MUU56150.1}; GN ORFNames=BGL73_02360 {ECO:0000313|EMBL:OPG44421.1}, D2C71_06230 GN {ECO:0000313|EMBL:QEF45294.1}, F7221_06820 GN {ECO:0000313|EMBL:MUU56150.1}; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210 {ECO:0000313|EMBL:OPG44421.1, ECO:0000313|Proteomes:UP000220272}; RN [1] {ECO:0000313|EMBL:OPG44421.1, ECO:0000313|Proteomes:UP000220272} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MGms167 {ECO:0000313|EMBL:OPG44421.1, RC ECO:0000313|Proteomes:UP000220272}; RX PubMed=28293542; DOI=.3389/fcimb.2017.00050; RA Munoz-Ramirez Z.Y., Mendez-Tenorio A., Kato I., Bravo M.M., Rizzato C., RA Thorell K., Torres R.C., Aviles-Jimenez F., Camorlinga M., Canzian F., RA Torres J.; RT "Whole Genome Sequence and Phylogenetic Analysis Show Helicobacter pylori RT Strains from Latin America Have Followed a Unique Evolution Pathway."; RL Front. Cell. Infect. Microbiol. 7:50-50(2017). RN [2] {ECO:0000313|EMBL:QEF45294.1, ECO:0000313|Proteomes:UP000321373} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G-Mx-2003-250 {ECO:0000313|EMBL:QEF45294.1, RC ECO:0000313|Proteomes:UP000321373}; RA Torres R.C., Torres J., Weimer B.C., Storey D.B., Becker M., Kong N.T., RA Huang C.B., Camorlinga M.; RT "Genome-Based Search for H. pylori Disease-Associated Genes in the Context RT of Different Populations."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:MUU56150.1, ECO:0000313|Proteomes:UP000483543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MHP18 {ECO:0000313|EMBL:MUU56150.1, RC ECO:0000313|Proteomes:UP000483543}; RX PubMed=31801839; RA Saranathan R., Levi M.H., Wattam A.R., Malek A., Asare E., Behin D.S., RA Pan D.H., Jacobs W.R., Szymczak W.A.; RT "Helicobacter pylori infections in the Bronx, New York: Surveying RT Antibiotic Susceptibility and Strain Lineage by Whole-genome Sequencing."; RL J. Clin. Microbiol. 0:0-0(2019). 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. {ECO:0000256|HAMAP-Rule:MF_01849}. 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 Evidence={ECO:0000256|HAMAP-Rule:MF_01849}; 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; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01849}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01849}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|HAMAP-Rule:MF_01849}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_01849}. CC -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving CC intermediate methylation of a conserved cysteine residue. CC {ECO:0000256|HAMAP-Rule:MF_01849}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. CC {ECO:0000256|ARBA:ARBA00007544, ECO:0000256|HAMAP-Rule:MF_01849}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01849}. 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; WADT01000019; MUU56150.1; -; Genomic_DNA. DR EMBL; MILK01000030; OPG44421.1; -; Genomic_DNA. DR EMBL; CP032048; QEF45294.1; -; Genomic_DNA. DR Proteomes; UP000220272; Unassembled WGS sequence. DR Proteomes; UP000321373; Chromosome. DR Proteomes; UP000483543; Unassembled WGS sequence. 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:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01849; RNA_methyltr_RlmN; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR040072; Methyltransferase_A. DR InterPro; IPR027492; RNA_MTrfase_RlmN. DR InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR30544; PTHR30544; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF006004; CHP00048; 1. DR SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1. DR TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01849}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01849}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_01849}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01849}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01849}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01849}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_01849, ECO:0000313|EMBL:OPG44421.1}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_01849}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP- KW Rule:MF_01849}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01849, ECO:0000313|EMBL:OPG44421.1}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849}. FT DOMAIN 119..278 FT /note="Radical_SAM" FT /evidence="ECO:0000259|Pfam:PF04055" FT REGION 173..174 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT REGION 226..228 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT ACT_SITE 89 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT ACT_SITE 345 FT /note="S-methylcysteine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT METAL 123 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT METAL 127 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT METAL 130 FT /note="Iron-sulfur (4Fe-4S-S-AdoMet)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 203 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 302 FT /note="S-adenosyl-L-methionine; via amide nitrogen and FT carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" SQ SEQUENCE 357 AA; 40759 MW; 037D84DB8ADDBD87 CRC64; MKASIYDFTL KELSQLLKPS FRAKQLYLWL YAKYKTSFKD MQNNFSKDFI AYLEQEFTLR TIEITHVRES VDGSKKYLFK SLRDNHTFEA VLLKMKDKKI DEETNAILEG EKYTVCVSCQ IGCQVGCAFC FTQKGGFVRN LKASEIIQQA LLIKEDNNLP IEKALNIVFM GMGEPLNNLD EVCKAVEIFN TGMQISPKRI TISTSGVADK IPILAGKNLG VQLAISLHAV DDKTRSSLMP LNKKYNIECV LNEVRKWPLE QRKRVMFEYL LIKDLNDSLD CAKKLLKLLN GIKSKVNLIL FNPHEGSKFE RPSLESARMF ADFLNSKGLL CTIRESKALD IEAACGQLRE KKLQQKI //