ID   NOVT_STRNV              Reviewed;         336 AA.
AC   Q9L9E8;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=dTDP-glucose 4,6-dehydratase;
DE            EC=4.2.1.46;
DE   AltName: Full=Novobiocin biosynthesis protein T;
GN   Name=novT;
OS   Streptomyces niveus (Streptomyces spheroides).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=193462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC   2449;
RX   PubMed=10770754; DOI=10.1128/aac.44.5.1214-1222.2000;
RA   Steffensky M., Muhlenweg A., Wang Z.X., Li S.M., Heide L.;
RT   "Identification of the novobiocin biosynthetic gene cluster of Streptomyces
RT   spheroides NCIB 11891.";
RL   Antimicrob. Agents Chemother. 44:1214-1222(2000).
RN   [2]
RP   REVIEW, AND POSSIBLE FUNCTION.
RX   PubMed=16868863; DOI=10.1055/s-2006-946699;
RA   Li S.M., Heide L.;
RT   "The biosynthetic gene clusters of aminocoumarin antibiotics.";
RL   Planta Med. 72:1093-1099(2006).
CC   -!- FUNCTION: dTDP-glucose 4,6-dehydratase involved in the generation of
CC       the deoxysugar in the novobiocin biosynthesis pathway, an aminocoumarin
CC       family antibiotic that targets bacterial DNA gyrases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC         + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477,
CC         ChEBI:CHEBI:57649; EC=4.2.1.46;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; novobiocin biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR   EMBL; AF170880; AAF67513.1; -; Genomic_DNA.
DR   RefSeq; WP_069626148.1; NZ_MDCR01000039.1.
DR   AlphaFoldDB; Q9L9E8; -.
DR   SMR; Q9L9E8; -.
DR   KEGG; ag:AAF67513; -.
DR   BioCyc; MetaCyc:MON-18087; -.
DR   UniPathway; UPA01035; -.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR   CDD; cd05246; dTDP_GD_SDR_e; 1.
DR   InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Lyase; NAD.
FT   CHAIN           1..336
FT                   /note="dTDP-glucose 4,6-dehydratase"
FT                   /id="PRO_0000424007"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
FT   BINDING         37..40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..64
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   336 AA;  36731 MW;  3699A7CD62B00BAE CRC64;
     MRILVTGGAG FIGSEFVRAT LRGTLPGSSG TQVTVLDKLT YSGNVLNLAP IADLRNYRFV
     RGDICDQDLV DDVVAGHDAI VHFAAETHVD RSIGSAASFV RTNAMGTQVL LEAASRHRLG
     RFVHISTDEV YGSIPEGAWD EESPVAPNAP YAAAKAAGDL LALAWHRTHG LDVVVTRCTN
     NYGPYQYPEK LIPLFTTNVM DGQQVPVYGE GHNRRQWLHV SDHCRAIQLV LLGGRAGEVY
     HIGGGTELTN LELAEQILKS CGAGWDMVRH VPDRPGHDFR YSLDTTKIRT ELGFSPRVAF
     ADGLVETVEW YRDNRAWWEP LKSPDEATGS PGDAGR