ID   A0A1M6I9X4_9BACT        Unreviewed;       357 AA.
AC   A0A1M6I9X4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=SAMN05444280_1167 {ECO:0000313|EMBL:SHJ31205.1};
OS   Tangfeifania diversioriginum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Tangfeifania.
OX   NCBI_TaxID=1168035 {ECO:0000313|EMBL:SHJ31205.1, ECO:0000313|Proteomes:UP000184050};
RN   [1] {ECO:0000313|EMBL:SHJ31205.1, ECO:0000313|Proteomes:UP000184050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27063 {ECO:0000313|EMBL:SHJ31205.1,
RC   ECO:0000313|Proteomes:UP000184050};
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}.
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; FQZE01000016; SHJ31205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6I9X4; -.
DR   STRING; 1168035.SAMN05444280_1167; -.
DR   Proteomes; UP000184050; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184050}.
FT   DOMAIN          12..327
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   357 AA;  41231 MW;  5C2B8F81878C3F15 CRC64;
     MVSKYENMKT ILITGGAGFI GSHVVRLFVN KYPDYKIVNL DKLTYAGNLA NLKDVENKPN
     YEFVKGDIVD GDFILQLFEE RQFDGVIHLA AESHVDRSIS NPTEFVYTNV IGTVNLLNAA
     KHIWKDDFSD KKFYHISTDE VYGSLGEEGI FTEETRYDPH SPYSASKASS DHFVRAYHDT
     FGLPVIISNC SNNYGSYQFP EKLIPLFINN IRNKKPLPVY GKGENVRDWL WVVDHARAID
     VIYHKGKTGD TYNIGGFNEW KNIDLIRTMC RVMDKKLGRE EGESEKLITY VKDRAGHDLR
     YAIDATKIKN ELGWEPSVQF EEGISKTIDW YLDNEEWMKN VTSGDYQKYY DKQYLNR
//