DMRMT_AMYMS
ID DMRMT_AMYMS Reviewed; 272 AA.
AC G0FUS0; O52570;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=27-O-demethylrifamycin SV methyltransferase {ECO:0000303|PubMed:12623077};
DE Short=DMRSV methyltransferase {ECO:0000303|PubMed:12623077};
DE EC=2.1.1.315 {ECO:0000269|PubMed:12623077};
GN OrderedLocusNames=RAM_03320 {ECO:0000312|EMBL:AEK39156.1};
OS Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=713604;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S699;
RX PubMed=9512878; DOI=10.1016/s1074-5521(98)90141-7;
RA August P.R., Tang L., Yoon Y.J., Ning S., Mueller R., Yu T.W., Taylor M.,
RA Hoffmann D., Kim C.G., Zhang X., Hutchinson C.R., Floss H.G.;
RT "Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the
RT molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis
RT mediterranei S699.";
RL Chem. Biol. 5:69-79(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S699;
RX PubMed=21914879; DOI=10.1128/jb.05819-11;
RA Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT "Whole genome sequence of the rifamycin B-producing strain Amycolatopsis
RT mediterranei S699.";
RL J. Bacteriol. 193:5562-5563(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=S699;
RX PubMed=12623077; DOI=10.1016/s0003-9861(03)00004-3;
RA Xu J., Mahmud T., Floss H.G.;
RT "Isolation and characterization of 27-O-demethylrifamycin SV
RT methyltransferase provides new insights into the post-PKS modification
RT steps during the biosynthesis of the antitubercular drug rifamycin B by
RT Amycolatopsis mediterranei S699.";
RL Arch. Biochem. Biophys. 411:277-288(2003).
CC -!- FUNCTION: Catalyzes the methylation of 27-O-demethylrifamycin SV
CC (DMRSV) to rifamycin SV. {ECO:0000269|PubMed:12623077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=27-O-demethylrifamycin SV + S-adenosyl-L-methionine = H(+) +
CC rifamycin SV + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44740,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84571, ChEBI:CHEBI:84572; EC=2.1.1.315;
CC Evidence={ECO:0000269|PubMed:12623077};
CC -!- ACTIVITY REGULATION: Slightly inhibited by Ca(2+) and Mg(2+). Strongly
CC inhibited by Zn(2+), Ni(2+) and Co(2+). {ECO:0000269|PubMed:12623077}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.0 uM for 27-O-demethylrifamycin SV
CC {ECO:0000269|PubMed:12623077};
CC KM=19.3 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12623077};
CC Note=kcat is 87 sec(-1). {ECO:0000269|PubMed:12623077};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:12623077};
CC -!- PATHWAY: Antibiotic biosynthesis; rifamycin B biosynthesis.
CC {ECO:0000269|PubMed:12623077}.
CC -!- SUBUNIT: Exists probably as a trimer. {ECO:0000269|PubMed:12623077}.
CC -!- DISRUPTION PHENOTYPE: Mutant loses its ability to produce rifamycin B,
CC but accumulates 27-O-demethylrifamycin SV (DMRSV) as the major new
CC metabolite, together with a small quantity of 27-O-demethyl-25-O-
CC desacetylrifamycin SV (DMDARSV). {ECO:0000269|PubMed:12623077}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. {ECO:0000305}.
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DR EMBL; AF040570; AAC01738.1; -; Genomic_DNA.
DR EMBL; CP002896; AEK39156.1; -; Genomic_DNA.
DR RefSeq; WP_013222580.1; NC_018266.1.
DR AlphaFoldDB; G0FUS0; -.
DR SMR; G0FUS0; -.
DR STRING; 713604.RAM_03320; -.
DR EnsemblBacteria; AEK39156; AEK39156; RAM_03320.
DR KEGG; amn:RAM_03320; -.
DR PATRIC; fig|713604.12.peg.689; -.
DR OMA; YHEVEGG; -.
DR OrthoDB; 1518440at2; -.
DR BioCyc; MetaCyc:MON-14112; -.
DR UniPathway; UPA01029; -.
DR Proteomes; UP000006138; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR020803; PKS_MeTfrase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SMART; SM00828; PKS_MT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..272
FT /note="27-O-demethylrifamycin SV methyltransferase"
FT /id="PRO_0000435820"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8KZ94"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8KZ94"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8KZ94"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8KZ94"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8KZ94"
FT CONFLICT 23
FT /note="L -> F (in Ref. 1; AAC01738)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 30261 MW; 4E672B5C5A3F11FC CRC64;
MTKPTPNEIG KGYDAFADLL DQLWGENLHH GYWDDESATL EEATTRLTDR LAGMLPLRAG
DRLLDIGCGN GEPAIRMATA NDVMVTGISI SEKQVERAND RAYKADVDDR VVFEYADAME
LPYPDASFDV VWALESLHHM PDRWHVIRQA ARVLRPGGRL ALGDFLLVPS PAGLEADAER
VREVGKGVVA VVSLDEYQAH LREAGLEPES AEDVSQYTRP SWTKAAERFE GLREQALQHI
EAAQFEVTLG RFRAFSEEPS LGYVLLTARK PD
