MYCE_MICGR
ID MYCE_MICGR Reviewed; 399 AA.
AC Q83WF2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Mycinamicin VI 2''-O-methyltransferase {ECO:0000305};
DE EC=2.1.1.238 {ECO:0000269|PubMed:19415708, ECO:0000269|PubMed:21884704};
DE AltName: Full=Mycinamicin biosynthesis protein E;
GN Name=mycE;
OS Micromonospora griseorubida.
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=28040;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12583909; DOI=10.1111/j.1574-6968.2003.tb11509.x;
RA Anzai Y., Saito N., Tanaka M., Kinoshita K., Koyama Y., Kato F.;
RT "Organization of the biosynthetic gene cluster for the polyketide macrolide
RT mycinamicin in Micromonospora griseorubida.";
RL FEMS Microbiol. Lett. 218:135-141(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND COFACTOR.
RC STRAIN=A11725;
RX PubMed=19415708; DOI=10.1002/cbic.200900088;
RA Li S., Anzai Y., Kinoshita K., Kato F., Sherman D.H.;
RT "Functional analysis of MycE and MycF, two O-methyltransferases involved in
RT the biosynthesis of mycinamicin macrolide antibiotics.";
RL ChemBioChem 10:1297-1301(2009).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=A11725;
RX PubMed=20158522; DOI=10.1111/j.1574-6968.2010.01899.x;
RA Tsukada S., Anzai Y., Li S., Kinoshita K., Sherman D.H., Kato F.;
RT "Gene targeting for O-methyltransferase genes, mycE and mycF, on the
RT chromosome of Micromonospora griseorubida producing mycinamicin with a
RT disruption cassette containing the bacteriophage phi C31 attB attachment
RT site.";
RL FEMS Microbiol. Lett. 304:148-156(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP ACTIVE SITES, AND MUTAGENESIS OF TYR-208; HIS-278 AND ILE-279.
RX PubMed=21884704; DOI=10.1016/j.jmb.2011.08.040;
RA Akey D.L., Li S., Konwerski J.R., Confer L.A., Bernard S.M., Anzai Y.,
RA Kato F., Sherman D.H., Smith J.L.;
RT "A new structural form in the SAM/metal-dependent o-methyltransferase
RT family: MycE from the mycinamicin biosynthetic pathway.";
RL J. Mol. Biol. 413:438-450(2011).
CC -!- FUNCTION: O-methyltransferase that catalyzes the conversion of
CC mycinamicin VI to mycinamicin III in the biosynthesis of mycinamicin, a
CC 16-membered macrolide antibiotic. {ECO:0000269|PubMed:19415708,
CC ECO:0000269|PubMed:21884704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mycinamicin VI + S-adenosyl-L-methionine = H(+) + mycinamicin
CC III + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31643,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:63308, ChEBI:CHEBI:63311; EC=2.1.1.238;
CC Evidence={ECO:0000269|PubMed:19415708, ECO:0000269|PubMed:21884704};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19415708, ECO:0000269|PubMed:21884704};
CC -!- PATHWAY: Antibiotic biosynthesis; mycinamicin biosynthesis.
CC {ECO:0000269|PubMed:19415708}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21884704}.
CC -!- DISRUPTION PHENOTYPE: No production of mycinamicin II and accumulation
CC of mycinamicin VI. {ECO:0000269|PubMed:20158522}.
CC -!- SIMILARITY: Belongs to the methyltransferase OleY/MycE family.
CC {ECO:0000305}.
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DR EMBL; AB089954; BAC57026.1; -; Genomic_DNA.
DR PDB; 3SSM; X-ray; 2.25 A; A/B/C/D=1-399.
DR PDB; 3SSN; X-ray; 2.39 A; A/B/C/D=1-399.
DR PDB; 3SSO; X-ray; 1.90 A; A/B/C/D/E/F=1-399.
DR PDBsum; 3SSM; -.
DR PDBsum; 3SSN; -.
DR PDBsum; 3SSO; -.
DR AlphaFoldDB; Q83WF2; -.
DR SMR; Q83WF2; -.
DR KEGG; ag:BAC57026; -.
DR BioCyc; MetaCyc:MON-18367; -.
DR BRENDA; 2.1.1.238; 7845.
DR UniPathway; UPA01019; -.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0102302; F:mycinamicin VI 2''-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008171; F:O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR040800; MycE_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF17843; MycE_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Magnesium; Metal-binding;
KW Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..399
FT /note="Mycinamicin VI 2''-O-methyltransferase"
FT /id="PRO_0000418457"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 202..208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 252..253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21884704"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21884704"
FT MUTAGEN 208
FT /note="Y->F: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:21884704"
FT MUTAGEN 278
FT /note="H->A,K,Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:21884704"
FT MUTAGEN 279
FT /note="I->V: Slightly increased catalytic activity."
FT /evidence="ECO:0000269|PubMed:21884704"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3SSN"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 135..155
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 294..303
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 305..309
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 326..337
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 352..356
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:3SSO"
FT STRAND 366..372
FT /evidence="ECO:0007829|PDB:3SSO"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:3SSO"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:3SSO"
SQ SEQUENCE 399 AA; 44809 MW; D608846BD0F5A012 CRC64;
MTAQTEFDEA TVQDVVRLAG GHDSELRELT QKYDPAMISR LLVAEILSRC PPPSNDTPVL
VELAIVHGSE RFRHFLRVVR DSPIRPVGAD EGFVGMLVEY ELTELLRELF GVTHERPAGV
RGTKLFPYLT DDEEAVEQIG TYLLAAQQGT EAVLAGCGSR KPDLSELSSR YFTPKFGFLH
WFTPHYDRHF RDYRNQQVRV LEIGVGGYKH PEWGGGSLRM WKSFFPRGQI YGLDIMDKSH
VDELRIRTIQ GDQNDAEFLD RIARRYGPFD IVIDDGSHIN AHVRTSFAAL FPHVRPGGLY
VIEDMWTAYW PGFGGQADPQ ECSGTSLGLL KSLIDAIQHQ ELPSDPNRSP GYVDRNIVGL
HVYHNVAFVE KGRNDEGGIP TWIPRDFESL VQASSGGAT
