ACL_RS01235

Uniprot: A9NEU7
Description: 23S rRNA (adenine(2503)-C(2))-methyltransferase RlmN
EC number: 2.1.1.192
Annotation score: 4 out of 5
Miscellaneous [CC]: MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue. {ECO:0000255|HAMAP-Rule:MF_01849}.
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01849}.; CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01849}.
Cofactor: COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_01849}; ; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_01849}
Enzyme regulation:
Function [CC]: FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. {ECO:0000255|HAMAP-Rule:MF_01849}.
Pathway:
Active site: ACT_SITE 89 89 Proton acceptor. {ECO:0000255|HAMAP-Rule:MF_01849}.; ACT_SITE 330 330 S-methylcysteine intermediate. {ECO:0000255|HAMAP-Rule:MF_01849}.
Binding site: BINDING 188 188 S-adenosyl-L-methionine. {ECO:0000255|HAMAP-Rule:MF_01849}.; BINDING 287 287 S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_01849}.
Calcium binding:
DNA binding:
Metal binding: METAL 109 109 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO:0000255|HAMAP-Rule:MF_01849}.; METAL 113 113 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO:0000255|HAMAP-Rule:MF_01849}.; METAL 116 116 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO:0000255|HAMAP-Rule:MF_01849}.
Nucleotide binding:
Site:
Gene names (primary): rlmN
Gene names (synonym):
Mass: 38,282
Subunit structure [CC]:
Gene ontology (GO): cytoplasm [GO:0005737]; 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; rRNA (adenine-C2-)-methyltransferase activity [GO:0070040]; rRNA binding [GO:0019843]; tRNA (adenine-C2-)-methyltransferase activity [GO:0002935]; tRNA binding [GO:0000049]; rRNA base methylation [GO:0070475]
Gene ontology IDs: GO:0000049; GO:0002935; GO:0005737; GO:0019843; GO:0046872; GO:0051539; GO:0070040; GO:0070475
Chain: CHAIN 1 338 Probable dual-specificity RNA methyltransferase RlmN. /FTId=PRO_0000349991.
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. {ECO:0000255|HAMAP-Rule:MF_01849}.
Protein families: Radical SAM superfamily, RlmN family
Coiled coil:
Domain [FT]:
Motif:
Region: REGION 156 157 S-adenosyl-L-methionine binding. {ECO:0000255|HAMAP-Rule:MF_01849}.; REGION 211 213 S-adenosyl-L-methionine binding. {ECO:0000255|HAMAP-Rule:MF_01849}.
EMBL: CP000896
ProteinModelPortal: A9NEU7
MEROPS:
EnsemblBacteria KO: ABX80877
UniPathway: K06941
CDD:
Gene3D:
HAMAP: 3.20.20.70
InterPro: MF_01849
PANTHER: IPR013785;IPR006638;IPR027492;IPR004383;IPR007197
PIRSF: PTHR30544
PRINTS: PIRSF006004
PROSITE:
Pfam:
ProDom: PF04055
SMART:
SUPFAM: SM00729
TIGRFAMs:

251470-252487(+)

>nucleotide sequence
ATGCTAATTTATGATTTAACATACGAAGAATTAGAAGAATTCATCGTAGAAAACGGCTAT
AAGAAATTTAGAGCCGATCAAATTTGGAACTGGCTCTATAAACAAAAAATAGAGGCGTTC
AGTGAAATGAATAACATCCCAGAGGACATCATTAAATTATTGAATGATAATTATACCTTT
GCAGGACTTGAAACAGTGATCAAAAATACCAGTGCAGATGGTACAATTAAGTTTTTATTT
GACTTAAAAGATGCGAATCTAATTGAAACGGTATTAATGAGTCATAACTATGGCATGAGT
GCCTGTGTGACTACTCAAGTAGGATGTAACATTGGATGTAGTTTTTGTGCATCTGGTGTA
TTAAAGAAAAAAAGAGACTTAACAGCAGGTGAAATTGTTGCACAAATCATTCGTGCAGAA
AAAGAATCTGGTGTGAGAGTGTCTAGTATTGTTATTATGGGTATTGGTGAACCATTTGAT
AACTATAAGAACTTTGTTAAATTTATTAGCATTGTAAATCACCCTAAAGGACTAGCAATT
GGTGCAAGACATATTACAGTGTCTACATCTGGTTTAGTACCTAAGATTAAAGAATTTGCT
CATTTAGGTATTCAAGTAAACTTAGCGGTTTCGCTACATGCACCGAATAATGAAATTAGA
TCTAAATTAATGAAAATCAATGATAGATTCAAAGTTGAAGAAGTCGTAGATGCAATCAAA
TACTATATTCATGTTACTAACAGAAGAGTTACAATTGAATATATTATGATTCAAGATTTA
AATGATAGTGTAGAAACTGCAGTAGAATTAGCTAAACTCTTAAAGGGTATGAATGTCTAT
GTGAATTTAATTCCATATAACACCGTTAAAGAAGCAGATTATCAAAGATCAAGTCTTGAG
AATCGTTTAGCATTCCACAAGACTTTAAAAGAACATAAAATCACTGCAATTTTAAGAAAA
GAACAAGGTCATGACATTAATGCTGCTTGTGGCCAATTAAGAAGTCAAAATCTATAA

>protein sequence
MLIYDLTYEELEEFIVENGYKKFRADQIWNWLYKQKIEAFSEMNNIPEDIIKLLNDNYTF
AGLETVIKNTSADGTIKFLFDLKDANLIETVLMSHNYGMSACVTTQVGCNIGCSFCASGV
LKKKRDLTAGEIVAQIIRAEKESGVRVSSIVIMGIGEPFDNYKNFVKFISIVNHPKGLAI
GARHITVSTSGLVPKIKEFAHLGIQVNLAVSLHAPNNEIRSKLMKINDRFKVEEVVDAIK
YYIHVTNRRVTIEYIMIQDLNDSVETAVELAKLLKGMNVYVNLIPYNTVKEADYQRSSLE
NRLAFHKTLKEHKITAILRKEQGHDINAACGQLRSQNL