REBMT_LENAE
ID REBMT_LENAE Reviewed; 283 AA.
AC Q8KZ94;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Demethylrebeccamycin-D-glucose O-methyltransferase;
DE EC=2.1.1.164 {ECO:0000269|PubMed:18502766};
DE AltName: Full=Rebeccamycin O-methyltransferase;
DE AltName: Full=Rebeccamycin sugar 4'-O-methyltransferase RebM;
GN Name=rebM;
OS Lentzea aerocolonigenes (Lechevalieria aerocolonigenes) (Saccharothrix
OS aerocolonigenes).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=68170;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RA Nishizawa T., Aldrich C.C., Sherman D.H.;
RT "Lechevalieria aerocolonigenes strain ATCC 39243 rebeccamycin biosynthetic
RT gene cluster.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16575939; DOI=10.1002/cbic.200500504;
RA Zhang C., Albermann C., Fu X., Peters N.R., Chisholm J.D., Zhang G.,
RA Gilbert E.J., Wang P.G., Van Vranken D.L., Thorson J.S.;
RT "RebG- and RebM-catalyzed indolocarbazole diversification.";
RL ChemBioChem 7:795-804(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 12-283 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF PRO-85; LEU-146; SER-148; HIS-150;
RP HIS-151 AND ASP-176.
RX PubMed=18502766; DOI=10.1074/jbc.m800503200;
RA Singh S., McCoy J.G., Zhang C., Bingman C.A., Phillips G.N., Thorson J.S.;
RT "Structure and mechanism of the rebeccamycin sugar 4'-O-methyltransferase
RT RebM.";
RL J. Biol. Chem. 283:22628-22636(2008).
CC -!- FUNCTION: Glycosyl O-methyltransferase that catalyzes the final step in
CC the biosynthesis of rebeccamycin, an indolocarbazole alkaloid that
CC inhibits topoisomerase 1. Has broad substrate specificity and functions
CC as glycosyl O-methyltransferase on a number of rebeccamycin analogs.
CC {ECO:0000269|PubMed:16575939, ECO:0000269|PubMed:18502766}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4'-demethylrebeccamycin + S-adenosyl-L-methionine = H(+) +
CC rebeccamycin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:27353,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:135511, ChEBI:CHEBI:595389; EC=2.1.1.164;
CC Evidence={ECO:0000269|PubMed:18502766};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:16575939,
CC ECO:0000269|PubMed:18502766};
CC pH dependence:
CC Optimum pH is 6.5-8. {ECO:0000269|PubMed:16575939,
CC ECO:0000269|PubMed:18502766};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16575939,
CC ECO:0000269|PubMed:18502766}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AB090952; BAC10678.1; -; Genomic_DNA.
DR PDB; 3BUS; X-ray; 2.65 A; A/B=12-283.
DR PDBsum; 3BUS; -.
DR AlphaFoldDB; Q8KZ94; -.
DR SMR; Q8KZ94; -.
DR KEGG; ag:BAC10678; -.
DR BRENDA; 2.1.1.164; 4340.
DR EvolutionaryTrace; Q8KZ94; -.
DR GO; GO:0102082; F:demethylrebeccamycin--D-glucose O-methyltransferase activity; IEA:UniProtKB-EC.
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 3D-structure; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..283
FT /note="Demethylrebeccamycin-D-glucose O-methyltransferase"
FT /id="PRO_0000415892"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:18502766,
FT ECO:0007744|PDB:3BUS"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:18502766,
FT ECO:0007744|PDB:3BUS"
FT BINDING 129..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:18502766,
FT ECO:0007744|PDB:3BUS"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:18502766,
FT ECO:0007744|PDB:3BUS"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:18502766"
FT SITE 150
FT /note="Important for catalysis"
FT MUTAGEN 85
FT /note="P->S: Reduces enzyme activity by 87%. Strongly
FT reduced affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:18502766"
FT MUTAGEN 146
FT /note="L->V: Reduces enzyme activity by 45%. Reduces
FT affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:18502766"
FT MUTAGEN 148
FT /note="S->A: Reduces enzyme activity by 50%."
FT /evidence="ECO:0000269|PubMed:18502766"
FT MUTAGEN 150
FT /note="H->A: Reduces enzyme activity by 95%. Slightly
FT reduced affinity for S-adenosyl-L-methionine. Loss of
FT enzyme activity; when associated with A-151."
FT /evidence="ECO:0000269|PubMed:18502766"
FT MUTAGEN 151
FT /note="H->A: Reduces enzyme activity by 80%. Strongly
FT reduced affinity for S-adenosyl-L-methionine. Loss of
FT enzyme activity; when associated with A-150."
FT /evidence="ECO:0000269|PubMed:18502766"
FT MUTAGEN 176
FT /note="D->A: Reduces enzyme activity by 90%. Strongly
FT reduced affinity for S-adenosyl-L-methionine."
FT /evidence="ECO:0000269|PubMed:18502766"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:3BUS"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3BUS"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:3BUS"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3BUS"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:3BUS"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:3BUS"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:3BUS"
FT STRAND 166..181
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 185..198
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:3BUS"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 233..243
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:3BUS"
FT HELIX 254..268
FT /evidence="ECO:0007829|PDB:3BUS"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:3BUS"
SQ SEQUENCE 283 AA; 30374 MW; 3A442B1545477CC6 CRC64;
MTESKSEGTA VAAPTPEEVR QMYDDFTDPF ARIWGENLHF GYWEDAGADV SVDDATDRLT
DEMIALLDVR SGDRVLDVGC GIGKPAVRLA TARDVRVTGI SISRPQVNQA NARATAAGLA
NRVTFSYADA MDLPFEDASF DAVWALESLH HMPDRGRALR EMARVLRPGG TVAIADFVLL
APVEGAKKEA VDAFRAGGGV LSLGGIDEYE SDVRQAELVV TSTVDISAQA RPSLVKTAEA
FENARSQVEP FMGAEGLDRM IATFRGLAEV PEAGYVLIGA RKP
