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Database: UniProt
Entry: T0V5Y3_9STRE
LinkDB: T0V5Y3_9STRE
Original site: T0V5Y3_9STRE 
ID   T0V5Y3_9STRE            Unreviewed;       348 AA.
AC   T0V5Y3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=HSISM1_1635 {ECO:0000313|EMBL:EQC77194.1};
OS   Streptococcus sp. HSISM1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC77194.1};
RN   [1] {ECO:0000313|EMBL:EQC77194.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISM1 {ECO:0000313|EMBL:EQC77194.1};
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT   Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL   PLoS ONE 8:E83418-E83418(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQC77194.1}.
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DR   EMBL; ASKI01000054; EQC77194.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0V5Y3; -.
DR   PATRIC; fig|1316408.3.peg.1189; -.
DR   eggNOG; COG1088; Bacteria.
DR   HOGENOM; CLU_007383_1_14_9; -.
DR   Proteomes; UP000015933; Chromosome.
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, ECO:0000313|EMBL:EQC77194.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          8..317
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   348 AA;  39180 MW;  94B4449CAFC57B37 CRC64;
     MSEYKHIIVT GGAGFIGSNF VHYVYNNHPD VHVTVLDKLT YAGNRANIEE ILGDRVELVV
     GDIADAELVD KLAAKADAIV HYAAESHNDN SLKDPSPFIY TNFVGTYTLL EAARKYDIRF
     HHVSTDEVYG DLPLREDLPG HGEGPGEKFT AETKYNPSSP YSSTKAASDL IVKAWVRSFG
     VKATISNCSN NYGPYQHIEK FIPRQITNIL SGIKPKLYGE GKNVRDWIHT NDHSTGVWAI
     LTKGRIGETY LIGADGEKNN KEVLELILEK MGQPKDAYDR VTDRAGHDLR YAIDSTKLRE
     ELGWEPQFTN FEAGLEDTIK WYTDHQDWWK AEKEAVEANY AKTQKVLK
//
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