Entry
Name
23S rRNA (adenine2085-N6)-dimethyltransferase;
ErmC' methyltransferase;
ermC methylase;
ermC 23S rRNA methyltransferase;
rRNA:m6A methyltransferase ErmC';
ErmC';
rRNA methyltransferase ErmC'
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:23S rRNA (adenine2085-N6)-dimethyltransferase
Reaction(IUBMB)
2 S-adenosyl-L-methionine + adenine2085 in 23S rRNA = 2 S-adenosyl-L-homocysteine + N6-dimethyladenine2085 in 23S rRNA [RN:
R10716 ]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:
C00019 ];
adenine2085 in 23S rRNA
Product
S-adenosyl-L-homocysteine [CPD:
C00021 ];
N6-dimethyladenine2085 in 23S rRNA
Comment
ErmC is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalysing the methylation of 23S rRNA at adenine2085.
History
EC 2.1.1.184 created 1976 as EC 2.1.1.48, part transferred 2010 to EC 2.1.1.184
Orthology
K00561 23S rRNA (adenine-N6)-dimethyltransferase
Genes
LYB : C3943_14160(erm-23S_rRNA)
SAU : SA0048(ermA) SA0766(ermA) SA1480(ermA) SA1951(ermA) SA2384(ermA)
SAV : SAV0052(ermA) SAV1655(ermA)
SAW : SAHV_0051(ermA) SAHV_1642(ermA)
SAH : SaurJH1_0039 SaurJH1_1747
SAJ : SaurJH9_0039 SaurJH9_1713
SAR : SAR0050(ermA1) SAR1735(ermA2)
SAA : SAUSA300_pUSA0307(ermC)
SUK : SAA6008_00830(ermA) SAA6008_01623(ermA_1)
SUW : SATW20_00430(ermA1) SATW20_16480(ermA2)
SAUZ : SAZ172_0044(ermA1) SAZ172_1667(ermA2)
SAUT : SAI1T1_2006330(ermA) SAI1T1_2011990(ermA) SAI1T1_2015840(ermA) SAI1T1_2019340(ermA)
SAUJ : SAI2T2_1006350(ermA) SAI2T2_1012010(ermA) SAI2T2_1015850(ermA) SAI2T2_1019350(ermA)
SAUK : SAI3T3_1006340(ermA) SAI3T3_1011990(ermA) SAI3T3_1015840(ermA) SAI3T3_1019340(ermA)
SAUQ : SAI4T8_1006330(ermA) SAI4T8_1012000(ermA) SAI4T8_1015850(ermA) SAI4T8_1019350(ermA)
SAUV : SAI7S6_1006340(ermA) SAI7S6_1012010(ermA) SAI7S6_1015850(ermA) SAI7S6_1019340(ermA)
SAUW : SAI5S5_1006300(ermA) SAI5S5_1011960(ermA) SAI5S5_1015790(ermA) SAI5S5_1019280(ermA) SAI5S5_20050(ermC)
SAUX : SAI6T6_1006310(ermA) SAI6T6_1011970(ermA) SAI6T6_1015800(ermA) SAI6T6_1019290(ermA)
SAUY : SAI8T7_1006340(ermA) SAI8T7_1012000(ermA) SAI8T7_1015830(ermA) SAI8T7_1019320(ermA)
SUY : SA2981_0052(ermA) SA2981_1614(ermA)
SAUC : CA347_1648(ermA5) CA347_49(ermA5)
SAUR : SABB_02575(ermA1) SABB_05250(ermA2)
SER : SERP1220(ermA-1) SERP1343(ermA-2) SERP2510(ermA-3)
SPET : CEP67_02750 CEP67_07740
MLEN : H3V22_01745(erm(B)) H3V22_01785(erm(B))
EAUR : NMQ00_15990(erm(B))
BAYD : BSPP4475_00515(erm)
SPW : SPCG_0172 SPCG_1323 SPCG_1327
SSK : SSUD12_1346 SSUD12_1565
SPAB : KQ224_08640(erm(B))
EFU : HMPREF0351_12804(ermA)
ESG : EsVE80_07090(ermB) EsVE80_p1-00130(ermB)
ECEC : NCTC12421_01166(erm)
ERAF : J9537_20525(erm(B))
TKR : C7K43_00275(erm-23S_rRNA)
ALOY : CJ190_008495(erm(A))
AMIT : DBT49_0000585(erm(A))
VFA : MM35RIKEN_22660(ermB)
VCOP : MM50RIKEN_19590(ermB)
BLAR : LC508_17745(erm(B))
CDF : CD630_20070(ermB) CD630_20100(ermB1)
PDC : CDIF630_02225(ermB1) CDIF630_02229(ermB2)
PDF : CD630DERM_20072(ermB)
PHX : KGNDJEFE_00529(erm_1) KGNDJEFE_01831(ermC') KGNDJEFE_02272(erm_2)
DDH : Desde_1644 Desde_1647
ETM : CE91St48_05660(ermB)
HALS : D7D81_05390 D7D81_13075(erm)
ECOU : M1R54_02815(erm(A)) M1R54_03150(erm(A))
AARG : Aargi30884_28740(ermB)
EHN : H9Q80_06575(erm(B)) H9Q80_07490(erm(B))
MBO : BQ2027_MB2010(erm(37))
CHAD : CHAD_02490(carB1) CHAD_04490(carB2)
CAUI : CAURIS_09035(carB2)
NFR : ERS450000_01376(rsmA_1)
NBR : O3I_025710 O3I_028830
NAD : NCTC11293_06190(ermC')
RCR : NCTC10994_01728(ksgA_2)
SCO : SCO6089(SCBAC1A6.13)
SAMB : SAM23877_5636(srm1) SAM23877_5808(ermSF)
SGX : H4W23_25560 H4W23_25565(erm)
SCOE : CP976_33775(erm(O))
MICS : C1N74_10880(erm-23S_rRNA)
AMAU : DSM26151_27220(rsmA)
LARI : KI794_07290(erm) KI794_14590(erm)
MPOR : KW076_01550(erm) KW076_08905(erm)
PALU : CJ193_003580(erm) CJ193_007655(erm)
BCAU : I6G59_05385(erm) I6G59_16080
AACI : ASQ49_06035 ASQ49_16540
ACTA : C1701_19120(erm-23S_rRNA)
ACTU : Actkin_05847(carB_2)
WNE : PIG85_07860(erm) PIG85_10605(erm)
AEY : CDG81_11200 CDG81_13135(rsmA)
PMUC : ING2E5A_0789(ermFU)
PGOL : K6V26_03560(erm(F))
COPR : Cop2CBH44_11580(ermC)
MALS : NWE55_16765(erm(F))
PTAN : CRYO30217_03560(ermD)
MIB : UY43_C0001G1083(ine151)
» show all
Taxonomy
Reference
Authors
Zhong P, Pratt SD, Edalji RP, Walter KA, Holzman TF, Shivakumar AG, Katz L
Title
Substrate requirements for ErmC' methyltransferase activity.
Journal
Sequence
Reference
Authors
Denoya C, Dubnau D
Title
Mono- and dimethylating activities and kinetic studies of the ermC 23 S rRNA methyltransferase.
Journal
J Biol Chem 264:2615-24 (1989)
Reference
Authors
Denoya CD, Dubnau D
Title
Site and substrate specificity of the ermC 23S rRNA methyltransferase.
Journal
Reference
Authors
Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C
Title
Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria.
Journal
Sequence
Reference
Authors
Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C
Title
The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism.
Journal
Sequence
Reference
Authors
Maravic G, Bujnicki JM, Feder M, Pongor S, Flogel M
Title
Alanine-scanning mutagenesis of the predicted rRNA-binding domain of ErmC' redefines the substrate-binding site and suggests a model for protein-RNA interactions.
Journal
Sequence
Other DBs
ExPASy - ENZYME nomenclature database: 2.1.1.184