MYCF_MICGR
ID MYCF_MICGR Reviewed; 254 AA.
AC Q49492; Q49493; Q79F70; Q83WF6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Mycinamicin III 3''-O-methyltransferase;
DE EC=2.1.1.237;
DE AltName: Full=Mycinamicin biosynthesis protein F;
GN Name=mycF;
OS Micromonospora griseorubida.
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Micromonospora.
OX NCBI_TaxID=28040;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=A11725;
RX PubMed=8163162; DOI=10.1016/0378-1119(94)90138-4;
RA Inouye M., Suzuki H., Takada Y., Muto N., Horinouchi S., Beppu T.;
RT "A gene encoding mycinamicin III O-methyltransferase from Micromonospora
RT griseorubida.";
RL Gene 141:121-124(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-254, AND FUNCTION.
RC STRAIN=A11725;
RX PubMed=7808395; DOI=10.1007/bf00302258;
RA Inouye M., Takada Y., Muto N., Horinouchi S., Beppu T.;
RT "Characterization and expression of a P-450-like mycinamicin biosynthesis
RT gene using a novel Micromonospora-Escherichia coli shuttle cosmid vector.";
RL Mol. Gen. Genet. 245:456-464(1994).
RN [4]
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 [5]
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).
CC -!- FUNCTION: O-methyltransferase that catalyzes the conversion of
CC mycinamicin III to mycinamicin IV in the biosynthesis of mycinamicin, a
CC 16-membered macrolide antibiotic. {ECO:0000269|PubMed:19415708,
CC ECO:0000269|PubMed:7808395, ECO:0000269|PubMed:8163162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=mycinamicin III + S-adenosyl-L-methionine = H(+) + mycinamicin
CC IV + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:31639,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:63308, ChEBI:CHEBI:63310; EC=2.1.1.237;
CC Evidence={ECO:0000269|PubMed:19415708};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19415708};
CC -!- PATHWAY: Antibiotic biosynthesis; mycinamicin biosynthesis.
CC {ECO:0000269|PubMed:19415708}.
CC -!- DISRUPTION PHENOTYPE: No production of mycinamicin II and accumulation
CC of mycinamicin III. {ECO:0000269|PubMed:20158522}.
CC -!- SIMILARITY: Belongs to the methyltransferase TylF/MycF family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC57022.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D16097; BAA03670.1; -; Genomic_DNA.
DR EMBL; AB089954; BAC57022.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D16098; BAA03673.1; -; Genomic_DNA.
DR PIR; S51595; S51595.
DR PDB; 4X7U; X-ray; 1.65 A; A/B=1-254.
DR PDB; 4X7V; X-ray; 1.45 A; A/B=1-254.
DR PDB; 4X7W; X-ray; 1.75 A; A/B=1-254.
DR PDB; 4X7X; X-ray; 1.75 A; A/B=1-254.
DR PDB; 4X7Y; X-ray; 1.40 A; A/B=1-254.
DR PDB; 4X7Z; X-ray; 1.44 A; A/B=1-254.
DR PDB; 4X81; X-ray; 1.59 A; A/B=1-254.
DR PDB; 4XVY; X-ray; 2.42 A; A/B=1-254.
DR PDB; 4XVZ; X-ray; 2.49 A; A/B/C/D=2-254.
DR PDBsum; 4X7U; -.
DR PDBsum; 4X7V; -.
DR PDBsum; 4X7W; -.
DR PDBsum; 4X7X; -.
DR PDBsum; 4X7Y; -.
DR PDBsum; 4X7Z; -.
DR PDBsum; 4X81; -.
DR PDBsum; 4XVY; -.
DR PDBsum; 4XVZ; -.
DR AlphaFoldDB; Q49492; -.
DR SMR; Q49492; -.
DR KEGG; ag:BAA03670; -.
DR BioCyc; MetaCyc:MON-18368; -.
DR BRENDA; 2.1.1.237; 7845.
DR UniPathway; UPA01019; -.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
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 DisProt; DP01356; -.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR008884; TylF_MeTrfase.
DR PANTHER; PTHR40036; PTHR40036; 1.
DR Pfam; PF05711; TylF; 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..254
FT /note="Mycinamicin III 3''-O-methyltransferase"
FT /id="PRO_0000418456"
FT BINDING 55..56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 83..87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 113..117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 189..190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9L9F2"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:4X7Y"
FT TURN 19..23
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4XVZ"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:4XVY"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4X7Y"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:4X7Y"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:4X7Y"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:4X7Y"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4X7Y"
SQ SEQUENCE 254 AA; 28612 MW; 91B4ADAF9F4A8B63 CRC64;
MSPSTGVELY LDLLKRTVSN FIYQDATHVA GLITEAAFVE EARESGEDYP TVAHTMIGMK
RLNNLQHCVE SALRDGVPGD VLETGVWRGG ACIFARGILK AYDVRDRTVW VADSFQGFPK
ITDDDHPMDA EMNLHQYNEA VDLPTSLATV QRNFSRYGLL DDQVRFLPGW FKDTMPTAPF
ERLAVLRMDG DSYGATMDVL THAYPRLSPG GFAIIDDYCI PACREAVHEY RDRHGISDEI
VEIDRQGVYW RRSA
