KEGG   ENZYME: 2.1.1.184Help
Entry
EC 2.1.1.184                Enzyme                                 

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
CIE: AN232_30680
PRG: RB151_016370(ermD)
PMP: Pmu_02850(erm(42))
BTO: WQG_970
BTRH: F543_22890
BTRA: F544_3050
NME: NMB0066(ermC)
VFG: C9I84_016
BSUT: BSUB_10005
BLH: BaLi_c28970(ermD)
BHA: BH0380
BCL: ABC3508
OIH: OB0921
LYB: C3943_14160(erm-23S_rRNA)
VPN: A21D_00889(ermD)
SAU: SA0048(ermA) SA0766(ermA) SA1480(ermA) SA1951(ermA) SA2384(ermA)
SAV: SAV0052(ermA) SAV1655(ermA)
SAW: SAHV_0051(ermA) SAHV_1642(ermA)
SAR: SAR0050(ermA1) SAR1735(ermA2)
SAA: SAUSA300_pUSA0307(ermC)
SUK: SAA6008_00830(ermA) SAA6008_01623(ermA_1)
SUC: ECTR2_126
SUW: SATW20_00430(ermA1) SATW20_16480(ermA2)
SAUG: SA268_2515
SAUZ: SAZ172_0044(ermA1) SAZ172_1667(ermA2)
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)
SHA: pSHaeB01(ermC)
SDT: SPSE_1800(ermA)
SPX: SPG_1241(ermB)
SPNN: T308_09065
SPV: SPH_1420
SNP: SPAP_0896(erm(TR))
SAGE: EN72_06990
SSB: SSUBM407_0952(ermB)
SOR: SOR_1880(ermB)
SIU: SII_0641(ermB)
SANC: SANR_1363(ermTR)
SLU: KE3_0212
LJH: LJP_0027c
EFA: EFA0007
EFC: EFAU004_01593(ermG)
EFAU: EFAU085_p3012(erm)
EFU: HMPREF0351_12804(ermA)
THL: TEH_23120
AOE: Clos_2851
HSC: HVS_13755(ermA1)
HSD: SD1D_1531
CDF: CD630_20070(ermB) CD630_20100(ermB)
PDC: CDIF630_02225(ermB1) CDIF630_02229(ermB2)
PDF: CD630DERM_20072(ermB)
PED: ING2D1G_1534(ermGT)
MTU: Rv1988(erm(37))
MTV: RVBD_1988
MTC: MT2042
MRA: MRA_2001
MTUR: CFBS_2095
MTD: UDA_1988
MTUC: J113_13695
MTUE: J114_10620
MTUH: I917_14015
MTUL: TBHG_01945
MTUT: HKBT1_2091
MTUU: HKBT2_2093
MBO: BQ2027_MB2010(erm(37))
MBB: BCG_2004
MBT: JTY_1999
MBX: BCGT_1798
MAF: MAF_19990
MMIC: RN08_2199
MVQ: MYVA_1303(erm(X))
MAB: MAB_2297
MABO: NF82_11485
CJK: jk1436(erm(X))
CUR: cu1922(erm(X))
CUA: CU7111_1847(erm(X))
CGY: CGLY_13945(ermA)
CSX: CSING_13175(ermA)
CMV: CMUST_04105(ermA)
CAMG: CAMM_02585
NFA: NFA_27210
NFR: ERS450000_01376(rsmA_1)
NCY: NOCYR_3185(carB)
RHU: A3Q40_02474(carB_2)
GBR: Gbro_3423
TPR: Tpau_0528
SCO: SCO6089(SCBAC1A6.13)
SBH: SBI_03035
SDV: BN159_2247(ermSF)
SLV: SLIV_07695(ermSF)
SAMB: SAM23877_5636(srm1) SAM23877_5808(ermSF)
STRD: NI25_08920
SMAL: SMALA_5962
SALF: SMD44_05855(ksgA)
SALJ: SMD11_1643
AUL: DCC27_002790(erm)
BCV: Bcav_1923
LMOI: VV02_04275
BLIN: BLSMQ_0384
MPH: MLP_23220
KFL: Kfla_5998
PSIM: KR76_04810
NDA: Ndas_2264
NAL: B005_4554
TCU: Tcur_0508
SRO: Sros_4551
SEN: SACE_0733(ermE)
AJA: AJAP_39985(ermA)
AMQ: AMETH_5559(ermE)
PSEA: WY02_07165
PSEH: XF36_07650
KAL: KALB_1436
ACTI: UA75_04315
ACAD: UA74_04215
AHG: AHOG_04070(carB1)
ACTA: C1701_19120(erm-23S_rRNA)
SAQ: Sare_4045
AFS: AFR_03150
CAI: Caci_6125
SNA: Snas_2596
BKS: BBKW_0982
TBI: Tbis_3490
CWO: Cwoe_0389
EYY: EGYY_26800(KsgA)
TTR: Tter_2586
PBT: ING2E5B_2269(ermF)
PMUC: ING2E5A_0789(ermFU)
PSAC: PSM36_1528(ermF)
RAG: B739_0033
DTN: DTL3_1144
MIB: UY43_C0001G1083(ine151)
 » show all
Taxonomy
Reference
1  [PMID:7543473]
  Authors
Zhong P, Pratt SD, Edalji RP, Walter KA, Holzman TF, Shivakumar AG, Katz L
  Title
Substrate requirements for ErmC' methyltransferase activity.
  Journal
J Bacteriol 177:4327-32 (1995)
DOI:10.1128/JB.177.15.4327-4332.1995
  Sequence
Reference
2  [PMID:2492520]
  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
3  [PMID:2440853]
  Authors
Denoya CD, Dubnau D
  Title
Site and substrate specificity of the ermC 23S rRNA methyltransferase.
  Journal
J Bacteriol 169:3857-60 (1987)
DOI:10.1128/JB.169.8.3857-3860.1987
Reference
4  [PMID:9585521]
  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
Biochemistry 37:7103-12 (1998)
DOI:10.1021/bi973113c
  Sequence
Reference
5  [PMID:10366505]
  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
J Mol Biol 289:277-91 (1999)
DOI:10.1006/jmbi.1999.2788
  Sequence
Reference
6  [PMID:12907737]
  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
Nucleic Acids Res 31:4941-9 (2003)
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.184
IUBMB Enzyme Nomenclature: 2.1.1.184
ExPASy - ENZYME nomenclature database: 2.1.1.184
BRENDA, the Enzyme Database: 2.1.1.184

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