DB code: D00076

RLCP classification 3.747.29000.21 : Transfer
CATH domain 3.40.50.150 : Rossmann fold Catalytic domain
1.10.8.100 : Helicase, Ruva Protein; domain 3
E.C. 2.1.1.184
CSA 1qam
M-CSA 1qam
MACiE

CATH domain Related DB codes (homologues)
3.40.50.150 : Rossmann fold S00637 S00639 S00262 S00261 S00291 S00412 D00075 D00079 D00080 D00082 D00083 D00823

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P13956 rRNA adenine N-6-methyltransferase
EC 2.1.1.184
Erythromycin resistance protein
Macrolide-lincosamide-streptogramin B resistance protein
NP_040407.1 (Protein)
NC_001376.1 (DNA/RNA sequence)
PF00398 (RrnaAD)
[Graphical View]
P21236 rRNA adenine N-6-methyltransferase
EC 2.1.1.184
ErmAM
Macrolide-lincosamide-streptogramin B resistance protein
PF00398 (RrnaAD)
[Graphical View]

KEGG enzyme name
23S rRNA (adenine2085-N6)-dimethyltransferase
ErmC' methyltransferase
ermC methylase
ermC 23S rRNA methyltransferase
rRNA:m6A methyltransferase ErmC'
ErmC'
rRNA methyltransferase ErmC'

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P21236 ERM_STRPN 2 S-adenosyl-L-methionine + adenine(2085) in 23S rRNA = 2 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(2085) in 23S rRNA.
P13956 ERM_BACSU 2 S-adenosyl-L-methionine + adenine(2085) in 23S rRNA = 2 S-adenosyl-L-homocysteine + N(6)-dimethyladenine(2085) in 23S rRNA.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00019 L00096 C00021 L00097
E.C.
Compound S-Adenosyl-L-methionine adenine2085 in 23S rRNA S-Adenosyl-L-homocysteine N6-dimethyladenine2085 in 23S rRNA
Type amino acids,amine group,nucleoside,sulfonium ion amine group,nucleic acids amino acids,amine group,nucleoside,sulfide group amine group,nucleic acids
ChEBI 67040
16680
57856
PubChem 34755
25246222
439155
1qamA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1qanA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:SAH Unbound
1qaoA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:SAM Unbound Unbound Unbound
1qaqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:SFG Unbound Unbound Unbound
2ercA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2ercB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yubA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1qamA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1qanA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1qaoA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1qaqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2ercA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2ercB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1yubA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [5] & [9]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1qamA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 101;TYR 104;PHE 163 ILE 102
1qanA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 101;TYR 104;PHE 163 ILE 102
1qaoA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 101;TYR 104;PHE 163 ILE 102
1qaqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 101;TYR 104;PHE 163 ILE 102
2ercA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 101;TYR 104;PHE 163 ILE 102
2ercB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 101;TYR 104;PHE 163 ILE 102
1yubA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASN 100;TYR 103;PHE 162 ILE 101 mutant I75T, S100N, H118R
1qamA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qanA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qaoA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qaqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ercA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2ercB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1yubA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[5]
p.287
[9]
Fig.4, p.102-106

References
[1]
Resource
Comments
Medline ID
PubMed ID 7543473
Journal J Bacteriol
Year 1995
Volume 177
Pages 4327-32
Authors Zhong P, Pratt SD, Edalji RP, Walter KA, Holzman TF, Shivakumar AG, Katz L
Title Substrate requirements for ErmC' methyltransferase activity.
Related PDB
Related UniProtKB
[2]
Resource
Comments STRUCTURE BY NMR
Medline ID 97331325
PubMed ID 9187657
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 483-9
Authors Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walter K, Holzman TF, Fesik SW
Title Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.
Related PDB 1yub
Related UniProtKB P21236
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 10-244
Medline ID 98254494
PubMed ID 9585521
Journal Biochemistry
Year 1998
Volume 37
Pages 7103-12
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.
Related PDB 2erc
Related UniProtKB P13956
[4]
Resource
Comments
Medline ID
PubMed ID 10508434
Journal J Med Chem
Year 1999
Volume 42
Pages 3852-9
Authors Hajduk PJ, Dinges J, Schkeryantz JM, Janowick D, Kaminski M, Tufano M, Augeri DJ, Petros A, Nienaber V, Zhong P, Hammond R, Coen M, Beutel B, Katz L, Fesik SW
Title Novel inhibitors of Erm methyltransferases from NMR and parallel synthesis.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 99296629
PubMed ID 10366505
Journal J Mol Biol
Year 1999
Volume 289
Pages 277-91
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.
Related PDB 1qam 1qan 1qao 1qaq
Related UniProtKB P13956
[6]
Resource
Comments
Medline ID
PubMed ID 11567089
Journal Protein Sci
Year 2001
Volume 10
Pages 1980-8
Authors Schubot FD, Chen CJ, Rose JP, Dailey TA, Dailey HA, Wang BC
Title Crystal structure of the transcription factor sc-mtTFB offers insights into mitochondrial transcription.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11959553
Journal Antimicrob Agents Chemother
Year 2002
Volume 46
Pages 1253-61
Authors Farrow KA, Lyras D, Polekhina G, Koutsis K, Parker MW, Rood JI
Title Identification of essential residues in the Erm(B) rRNA methyltransferase of Clostridium perfringens.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11763974
Journal J Mol Microbiol Biotechnol
Year 2002
Volume 4
Pages 93-9
Authors Bujnicki JM, Blumenthal RM, Rychlewski L
Title Sequence analysis and structure prediction of 23S rRNA:m1G methyltransferases reveals a conserved core augmented with a putative Zn-binding domain in the N-terminus and family-specific elaborations in the C-terminus.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 12946350
Journal J Mol Biol
Year 2003
Volume 332
Pages 99-109
Authors Maravic G, Feder M, Pongor S, Flogel M, Bujnicki JM
Title Mutational analysis defines the roles of conserved amino acid residues in the predicted catalytic pocket of the rRNA:m6A methyltransferase ErmC'.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 15114858
Journal Folia Microbiol (Praha)
Year 2004
Volume 49
Pages 3-7
Authors Maravic G, Bujnicki JM, Flogel M
Title Mutational analysis of basic residues in the N-terminus of the rRNA:m6A methyltransferase ErmC'.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 15136037
Journal J Mol Biol
Year 2004
Volume 339
Pages 337-53
Authors O'Farrell HC, Scarsdale JN, Rife JP
Title Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 15929997
Journal Protein Sci
Year 2005
Volume 14
Pages 1472-84
Authors Constantine KL, Krystek SR, Healy MD, Doyle ML, Siemers NO, Thanassi J, Yan N, Xie D, Goldfarb V, Yanchunas J, Tao L, Dougherty BA, Farmer BT 2nd
Title Structural and functional characterization of CFE88: evidence that a conserved and essential bacterial protein is a methyltransferase.
Related PDB
Related UniProtKB

Comments
According to the literature [9], the catalytic residues of this enzyme is nearly the same as that of Modification methylase TaqI (D00080 in EzCatDB), suggesting that it has a similar mechanism to that.

Created Updated
2004-05-06 2012-10-03