ID   A0A1N6ITQ7_9FLAO        Unreviewed;       359 AA.
AC   A0A1N6ITQ7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05444409_2990 {ECO:0000313|EMBL:SIO35383.1};
OS   Epilithonimonas zeae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Epilithonimonas.
OX   NCBI_TaxID=1416779 {ECO:0000313|EMBL:SIO35383.1, ECO:0000313|Proteomes:UP000185207};
RN   [1] {ECO:0000313|Proteomes:UP000185207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27623 {ECO:0000313|Proteomes:UP000185207};
RA   Varghese N., Submissions S.;
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; FSRK01000002; SIO35383.1; -; Genomic_DNA.
DR   RefSeq; WP_074236124.1; NZ_FSRK01000002.1.
DR   AlphaFoldDB; A0A1N6ITQ7; -.
DR   STRING; 1416779.SAMN05444409_2990; -.
DR   OrthoDB; 8967463at2; -.
DR   Proteomes; UP000185207; Unassembled WGS sequence.
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          5..330
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   359 AA;  40848 MW;  4EC6D04E1E31A700 CRC64;
     MKNIIITGGA GFIGSHVVRE FVKNNPDSKI INLDALTYAG NLENLKDIEN EPNYVFEKAD
     ITKPEELRKV FEKYNPDAVV HLAAESHVDR SITDPNAFIN TNVNGTANLL NLCIEFWTLN
     PDHTHGRFPN EPRKNLFYHV STDEVYGSLG ETGFFLETTP YDPQSPYSAS KAASDHLVRA
     YGNTYGMPFI LSNCSNNYGP NHFPEKLIPL CISNILNEKP LPIYGDGKYT RDWLFVIDHA
     KAIHQIFNES KTGETYNIGG FNEWQNIDLV KELIKQLDAK LGKPEGYSEK LITYVKDRPG
     HDKRYAIDAS KLNKDLGWRP SVTFEEGLGK TIDWFLENKE WLDNVTSGDY QKYYEGQYS
//