ID   SPNS_SACSN              Reviewed;         249 AA.
AC   Q9ALP0;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-dimethyltransferase {ECO:0000303|PubMed:18345667};
DE            EC=2.1.1.324 {ECO:0000305|PubMed:18345667};
GN   Name=spnS {ECO:0000303|PubMed:11358695};
OS   Saccharopolyspora spinosa.
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=60894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=11358695; DOI=10.1016/s1074-5521(01)00029-1;
RA   Waldron C., Matsushima P., Rosteck P.R. Jr., Broughton M.C., Turner J.,
RA   Madduri K., Crawford K.P., Merlo D.J., Baltz R.H.;
RT   "Cloning and analysis of the spinosad biosynthetic gene cluster of
RT   Saccharopolyspora spinosa.";
RL   Chem. Biol. 8:487-499(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC   STRAIN=NRRL 18537;
RX   PubMed=18345667; DOI=10.1021/ja0771383;
RA   Hong L., Zhao Z., Melancon C.E. III, Zhang H., Liu H.W.;
RT   "In vitro characterization of the enzymes involved in TDP-D-forosamine
RT   biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa.";
RL   J. Am. Chem. Soc. 130:4954-4967(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of forosamine ((4-
CC       dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly
CC       deoxygenated sugar component of several bioactive natural products such
CC       as the insecticidal spinosyns A and D (PubMed:11358695,
CC       PubMed:18345667). Catalyzes the dimethylation of the C-4 amino group
CC       from dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-glucose to yield dTDP-D-
CC       forosamine (PubMed:18345667). {ECO:0000269|PubMed:11358695,
CC       ECO:0000269|PubMed:18345667}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-amino-2,3,4,6-tetradeoxy-alpha-D-erythro-hexopyranose +
CC         2 S-adenosyl-L-methionine = dTDP-alpha-D-forosamine + 2 H(+) + 2 S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:49148, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90945,
CC         ChEBI:CHEBI:90947; EC=2.1.1.324;
CC         Evidence={ECO:0000305|PubMed:18345667};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:18345667};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18345667}.
CC   -!- SIMILARITY: Belongs to the methyltransferase TylM1/DesVI family.
CC       {ECO:0000305}.
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DR   EMBL; AY007564; AAG23280.1; -; Genomic_DNA.
DR   RefSeq; WP_044574799.1; NZ_PJNB01000001.1.
DR   AlphaFoldDB; Q9ALP0; -.
DR   SMR; Q9ALP0; -.
DR   STRING; 994479.GL877879_gene4839; -.
DR   KEGG; ag:AAG23280; -.
DR   BioCyc; MetaCyc:MON-16624; -.
DR   BRENDA; 2.1.1.324; 13744.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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   Magnesium; Metal-binding; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..249
FT                   /note="dTDP-4-amino-2,3,4,6-tetradeoxy-D-glucose N,N-
FT                   dimethyltransferase"
FT                   /id="PRO_0000444371"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZGH6"
FT   BINDING         59
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZGH6"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZGH6"
FT   BINDING         102..103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZGH6"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZGH6"
FT   BINDING         178..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZGH6"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ZGH6"
SQ   SEQUENCE   249 AA;  27669 MW;  A5985504E32EAFCE CRC64;
     MSRVSDTFAE TSSVYSPDHA DIYDAIHSAR GRDWAAEAGE VVQLVRTRLP EAQSLLDVAC
     GTGAHLERFR AEYAKVAGLE LSDAMREIAI RRVPEVPIHI GDIRDFDLGE PFDVITCLCF
     TAAYMRTVDD LRRVTRNMAR HLAPGGVAVI EPWWFPDKFI DGFVTGAVAH HGERVISRLS
     HSVLEGRTSR MTVRYTVAEP TGIRDFTEFE ILSLFTEDEY TAALEDAGIR AEYLPGAPNG
     RGLFVGIRN