ID   A0A1M7NC03_9FLAO        Unreviewed;       350 AA.
AC   A0A1M7NC03;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
DE            EC=4.2.1.46 {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
GN   ORFNames=SAMN05720268_2038 {ECO:0000313|EMBL:SHN00759.1};
OS   Polaribacter sp. KT 15.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1896175 {ECO:0000313|EMBL:SHN00759.1, ECO:0000313|Proteomes:UP000190644};
RN   [1] {ECO:0000313|EMBL:SHN00759.1, ECO:0000313|Proteomes:UP000190644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT 15 {ECO:0000313|EMBL:SHN00759.1,
RC   ECO:0000313|Proteomes:UP000190644};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001539,
CC         ECO:0000256|RuleBase:RU004473};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911,
CC         ECO:0000256|RuleBase:RU004473};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. dTDP-glucose dehydratase subfamily.
CC       {ECO:0000256|ARBA:ARBA00008178, ECO:0000256|RuleBase:RU004473}.
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DR   EMBL; LT670850; SHN00759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7NC03; -.
DR   Proteomes; UP000190644; Chromosome i.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR   CDD; cd05246; dTDP_GD_SDR_e; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01181; dTDP_gluc_dehyt; 1.
DR   PANTHER; PTHR43000:SF7; DTDP-D-GLUCOSE 4,6-DEHYDRATASE; 1.
DR   PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU004473}; NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          6..320
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   350 AA;  40056 MW;  66A8A62BEC58A514 CRC64;
     MSKKILITGG AGFIGSHVVR LFVNNYPNYQ IFNLDALTYA GNLENLTDVE SSANYTFLKG
     DITDEDYIKS IFETHQFDNV IHLAAESHVD RSITDPLAFA KTNILGTMIL LNAFKNLWQD
     NWQDKLFYHV STDEVYGTLG ETGLFTESTS YDPNSPYSAS KASSDHFVRA YGETYGLPYV
     ISNCSNNYGA NQFPEKLIPL FINNIINNKS LPVYGDGKYT RDWLYVLDHA IAIDLVFHKG
     KNEETYNIGG FNEWQNIDLI KLLCVQMDKK LGRKEGESEK LITYVKDRPG HDLRYAIDAS
     KINKELGWRP SVTFEQGLSK TIDWYLSNIE WMERIVSGAY EDYYQNQYTK
//