DESVI_STRVZ
ID DESVI_STRVZ Reviewed; 237 AA.
AC Q9ZGH6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose N,N-dimethyltransferase {ECO:0000305|PubMed:12119032};
DE EC=2.1.1.234 {ECO:0000269|PubMed:12119032};
GN Name=desVI {ECO:0000312|EMBL:AAC68678.1};
OS Streptomyces venezuelae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=54571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 15439 / DSM 41110 / IMRU3627 / M-2140;
RX PubMed=9770448; DOI=10.1073/pnas.95.21.12111;
RA Xue Y., Zhao L., Liu H.W., Sherman D.H.;
RT "A gene cluster for macrolide antibiotic biosynthesis in Streptomyces
RT venezuelae: architecture of metabolic diversity.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12111-12116(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12119032; DOI=10.1021/bi020245j;
RA Chen H., Yamase H., Murakami K., Chang C.W., Zhao L., Zhao Z., Liu H.W.;
RT "Expression, purification, and characterization of two N,N-
RT dimethyltransferases, tylM1 and desVI, involved in the biosynthesis of
RT mycaminose and desosamine.";
RL Biochemistry 41:9165-9183(2002).
RN [3] {ECO:0007744|PDB:3BXO}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE AND UDP-BENZENE, AND SUBUNIT.
RX PubMed=18327916; DOI=10.1021/bi800063j;
RA Burgie E.S., Holden H.M.;
RT "Three-dimensional structure of DesVI from Streptomyces venezuelae: a sugar
RT N,N-dimethyltransferase required for dTDP-desosamine biosynthesis.";
RL Biochemistry 47:3982-3988(2008).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase involved
CC in the biosynthesis of desosamine, found in certain macrolide
CC antibiotics such as erthyromycin, azithromycin, clarithromycin, and
CC methymycin. Catalyzes the last step in the biosynthesis of dTDP-
CC desosamine, i.e. the N,N-dimethylation of the 3-amino group of dTDP-3-
CC amino-3,4,6-trideoxy-alpha-D-glucose. {ECO:0000269|PubMed:12119032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose + 2 S-adenosyl-L-
CC methionine = dTDP-alpha-D-desosamine + 2 H(+) + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:31759, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:63260,
CC ChEBI:CHEBI:63262; EC=2.1.1.234;
CC Evidence={ECO:0000269|PubMed:12119032};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31760;
CC Evidence={ECO:0000305|PubMed:12119032};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=307.4 uM for dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose
CC {ECO:0000269|PubMed:12119032};
CC KM=276.6 uM for dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose
CC {ECO:0000269|PubMed:12119032};
CC Note=kcat is 92 min(-1) with dTDP-3-amino-3,4,6-trideoxy-alpha-D-
CC glucopyranose as substrate. kcat is 4.2 min(-1) with dTDP-3-amino-
CC 3,6-dideoxy-alpha-D-glucopyranose as substrate.
CC {ECO:0000269|PubMed:12119032};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:9770448}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12119032,
CC ECO:0000269|PubMed:18327916}.
CC -!- SIMILARITY: Belongs to the methyltransferase TylM1/DesVI family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF079762; AAC68678.1; -; Genomic_DNA.
DR RefSeq; WP_055641632.1; NZ_CP013129.1.
DR PDB; 3BXO; X-ray; 2.00 A; A/B=1-237.
DR PDBsum; 3BXO; -.
DR AlphaFoldDB; Q9ZGH6; -.
DR SMR; Q9ZGH6; -.
DR KEGG; ag:AAC68678; -.
DR OrthoDB; 1515497at2; -.
DR BioCyc; MetaCyc:MON-16954; -.
DR BRENDA; 2.1.1.234; 6106.
DR EvolutionaryTrace; Q9ZGH6; -.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..237
FT /note="dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucopyranose
FT N,N-dimethyltransferase"
FT /id="PRO_0000418452"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18327916"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18327916"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18327916,
FT ECO:0007744|PDB:3BXO"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18327916,
FT ECO:0007744|PDB:3BXO"
FT BINDING 67
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18327916,
FT ECO:0007744|PDB:3BXO"
FT BINDING 89..90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18327916,
FT ECO:0007744|PDB:3BXO"
FT BINDING 105
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:18327916,
FT ECO:0007744|PDB:3BXO"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18327916"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18327916"
FT BINDING 165..169
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18327916"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18327916"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:3BXO"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3BXO"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:3BXO"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3BXO"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:3BXO"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3BXO"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:3BXO"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 161..172
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 175..186
FT /evidence="ECO:0007829|PDB:3BXO"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 190..201
FT /evidence="ECO:0007829|PDB:3BXO"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:3BXO"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3BXO"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:3BXO"
SQ SEQUENCE 237 AA; 25979 MW; 156E67A0E7406AE8 CRC64;
MYEVDHADVY DLFYLGRGKD YAAEASDIAD LVRSRTPEAS SLLDVACGTG THLEHFTKEF
GDTAGLELSE DMLTHARKRL PDATLHQGDM RDFRLGRKFS AVVSMFSSVG YLKTTEELGA
AVASFAEHLE PGGVVVVEPW WFPETFADGW VSADVVRRDG RTVARVSHSV REGNATRMEV
HFTVADPGKG VRHFSDVHLI TLFHQAEYEA AFTAAGLRVE YLEGGPSGRG LFVGVPA
