ID W9T0D6_9PSED Unreviewed; 357 AA.
AC W9T0D6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:EXF44067.1};
GN ORFNames=BAY1663_03519 {ECO:0000313|EMBL:EXF44067.1};
OS Pseudomonas sp. BAY1663.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF44067.1, ECO:0000313|Proteomes:UP000019475};
RN [1] {ECO:0000313|EMBL:EXF44067.1, ECO:0000313|Proteomes:UP000019475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF44067.1,
RC ECO:0000313|Proteomes:UP000019475};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of Pseudomonas sp. BAY1663.";
RL Submitted (DEC-2013) 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 -!- 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:EXF44067.1}.
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DR EMBL; AZSV01000057; EXF44067.1; -; Genomic_DNA.
DR RefSeq; WP_037042455.1; NZ_AZSV01000057.1.
DR AlphaFoldDB; W9T0D6; -.
DR STRING; 1439940.BAY1663_03519; -.
DR PATRIC; fig|1439940.3.peg.3484; -.
DR eggNOG; COG1088; Bacteria.
DR OrthoDB; 9803010at2; -.
DR Proteomes; UP000019475; 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:UP000019475}.
FT DOMAIN 4..326
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 357 AA; 40061 MW; 9AF12C78D894C560 CRC64;
MRILVTGGAG FIGSALIRHL ILDTEHSVLN LDKLTYAGNL ESLASVEDNP RYQFLQADIA
DRERVSEALL DFQPDAVMHL AAESHVDRSI DGPAEFIQTN IVGTYQLLEA TRAYWQSLPA
ERRAAFRFHH ISTDEVYGDL HGVDDLFTET TPYAPSSPYS ASKASSDHLV RAWQRTYGLP
VLVTNCSNNY GPFHFPEKLI PLVILNALDG KPLPVYGDGS QIRDWLFVED HARALLKVVS
EGEVGETYNI GGHNEQKNID VVRGICALLE ELAPSKPAGL ARYEDLITFV KDRPGHDLRY
AIDAGKIERE LGWVPQETFQ SGLRKTVQWY LDNLEWCRRV QDGSYQRERL GALENIA
//
