ID K9BVR5_ACINO Unreviewed; 410 AA. AC K9BVR5; A0A241YR17; A0A334ABW9; DT 06-FEB-2013, integrated into UniProtKB/TrEMBL. DT 06-FEB-2013, sequence version 1. DT 22-FEB-2023, entry version 58. 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:SSV49916.1}; GN ORFNames=AE32_00515 {ECO:0000313|EMBL:KDM58511.1}, GD578_02505 GN {ECO:0000313|EMBL:QGA42841.1}, H0S59_02695 GN {ECO:0000313|EMBL:QPF41556.1}, SAMEA104305365_02295 GN {ECO:0000313|EMBL:SSV49916.1}; OS Acinetobacter nosocomialis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=106654 {ECO:0000313|EMBL:SSV49916.1, ECO:0000313|Proteomes:UP000252392}; RN [1] {ECO:0000313|EMBL:KDM58511.1, ECO:0000313|Proteomes:UP000027208} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIDMC 57 {ECO:0000313|EMBL:KDM58511.1, RC ECO:0000313|Proteomes:UP000027208}; RG The Broad Institute Genomics Platform; RG The Broad Institute Genome Sequencing Center for Infectious Disease; RA Murphy C., Cosimi L., Cerqueira G., Feldgarden M., Earl A., Spencer M.D., RA Fodor A., Sautter R.L., Hung D., Onderdonk A.B., Ernst C., Delaney M., RA DuBois A., Young S.K., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., Pearson M., Poon T.W., Priest M., RA Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Acinetobacter baumanii BIDMC 57."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SSV49916.1, ECO:0000313|Proteomes:UP000252392} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4300STDY7045889 {ECO:0000313|EMBL:SSV49916.1, RC ECO:0000313|Proteomes:UP000252392}; RG Pathogen Informatics; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000325778} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AC1530 {ECO:0000313|Proteomes:UP000325778}; RA Mohd Rani F., Alattraqchi A.G., A Rahman N.I., Ismail S., Clarke S., RA Yeo C.C.; RT "Genome sequence of multidrug resistant Acinetobacter nosocomialis AC1530 RT from Terengganu, Malaysia."; RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:QPF41556.1, ECO:0000313|Proteomes:UP000594600} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WM98B {ECO:0000313|EMBL:QPF41556.1, RC ECO:0000313|Proteomes:UP000594600}; RA Ghaly T.M., Sajjad A., Tetu S.G., Gillings M.R.; RT "A family of multi-drug resistance mega-plasmids in Acinetobacter RT species."; RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:QGA42841.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AC1530 {ECO:0000313|EMBL:QGA42841.1}; RA Alattraqchi A.G., Mohd Rani F., A. Rahman N.I., Ismail S., Cleary D.W., RA Clarke S.C., Yeo C.C.; RT "Complete Genome Sequencing of Acinetobacter baumannii AC1633 and RT Acinetobacter nosocomialis AC1530 Unveils a Large Multidrug-Resistant RT Plasmid Encoding the NDM-1 and OXA-58 Carbapenemases."; RL MSphere 6:0-0(2021). 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; JMUI01000001; KDM58511.1; -; Genomic_DNA. DR EMBL; CP045560; QGA42841.1; -; Genomic_DNA. DR EMBL; CP059078; QPF41556.1; -; Genomic_DNA. DR EMBL; UFOY01000003; SSV49916.1; -; Genomic_DNA. DR RefSeq; WP_002053401.1; NZ_VYTL01000001.1. DR AlphaFoldDB; K9BVR5; -. DR STRING; 106654.B7L44_18115; -. DR EnsemblBacteria; OTL16975; OTL16975; B9X80_01765. DR EnsemblBacteria; PVA02618; PVA02618; DC362_13420. DR GeneID; 60877215; -. DR Proteomes; UP000027208; Unassembled WGS sequence. DR Proteomes; UP000252392; Unassembled WGS sequence. DR Proteomes; UP000325778; Chromosome. DR Proteomes; UP000594600; Chromosome. 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 CDD; cd01335; Radical_SAM; 1. DR Gene3D; 1.10.150.530; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 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; 23S RRNA METHYLTRANSFERASE; 1. DR PANTHER; PTHR30544:SF5; RADICAL_SAM DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF006004; CHP00048; 1. DR SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1. DR PROSITE; PS51918; RADICAL_SAM; 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}; 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}; tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849}. FT DOMAIN 130..373 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" FT REGION 7..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 120 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT ACT_SITE 378 FT /note="S-methylcysteine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 144 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 148 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 151 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 200..201 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 232 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 254..256 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" FT BINDING 335 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01849" SQ SEQUENCE 410 AA; 45756 MW; 2E98CD9213296A88 CRC64; MSSAVVVSSE NLDGQQQSSS TPASPAAEKV NLLGMSRAQL EKFFEDIGEK KFRAGQVMKW IHQYFVTDFA EMTNISGKLR AKLEQICEIK APEVVHRHYS KDGTRKWVFR VGEGSGSLVE TVLIPAEDKT GSRKTLCISS QVGCALDCSF CSTGKQGFQR DLTPDEIIGQ LWMANYSYME EVPVAERERS VTNVVMMGMG EPLLNYDAVL SSMHIMLDDF AYGMSKRRVT LSTSGVVPKI DQLAQDIDVA LAISLHAPND ELRNELVPIN KKYPLAQLIA ACQRYIAKDG NESARKHVTI EYVMLEGVND QPEHAQQLLK LLKNLPSKIN LIPFNPFPHA PYGRSSRNRI ISFQKTLSDA GFVCTIRQTR GDDIDAACGQ LVGQVADRTR RAEQWQKKVA QRQEILRTQG //