ID A0A345ZI71_9GAMM Unreviewed; 350 AA.
AC A0A345ZI71;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 Name=rfbB {ECO:0000313|EMBL:AXK71446.1};
GN ORFNames=DWG18_03475 {ECO:0000313|EMBL:AXK71446.1};
OS Lysobacter sp. TY2-98.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=2290922 {ECO:0000313|EMBL:AXK71446.1, ECO:0000313|Proteomes:UP000254438};
RN [1] {ECO:0000313|EMBL:AXK71446.1, ECO:0000313|Proteomes:UP000254438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TY2-98 {ECO:0000313|EMBL:AXK71446.1,
RC ECO:0000313|Proteomes:UP000254438};
RA Kim S.-G., Park A.-Y., Lee Y.-J.;
RT "Lysobacter sp. nov. isolated from a farm soil.";
RL Submitted (AUG-2018) 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; CP031413; AXK71446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345ZI71; -.
DR KEGG; lyt:DWG18_03475; -.
DR OrthoDB; 9803010at2; -.
DR Proteomes; UP000254438; 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; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR43000:SF47; DTDP-GLUCOSE 4,6-DEHYDRATASE 2; 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:AXK71446.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000254438}.
FT DOMAIN 5..322
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 350 AA; 38830 MW; 352B3EC2427C8D95 CRC64;
MTTWLVTGGA GFIGGNFVLD AVRRGIRIIN LDALTYAGNL DTLSSLDSDA NHVFVQGDIG
DATLIERLLA EYRPDAIVNF AAESHVDRSI DGPAAFVHTN VVGTLNLLEK ARDYWRALDA
PARDAFRFLH VSTDEVYGSL GDEGKFTETT PYAPNSPYSA SKAASDHLVR AFHHTYGLPV
LTTNCSNNYG PFQFPEKLVP LIIARALRGE PLPVYGDGRN VRDWLFVGDH CAAIRRVLEA
GRVGETYNVG GNAERENIEV VRAICRLLDA KRPLADGRPR ESLITFVADR PGHDRRYAID
ASKIEHELGW SPTLTFEQGI EHTVDWYLDH QAWVERVLDG SYRLERIGQA
//
