ID A0A1Y0MYE0_9FLAO Unreviewed; 349 AA.
AC A0A1Y0MYE0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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 ORFNames=BTO07_08120 {ECO:0000313|EMBL:ARV15118.1};
OS Polaribacter sp. SA4-12.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1312072 {ECO:0000313|EMBL:ARV15118.1, ECO:0000313|Proteomes:UP000195470};
RN [1] {ECO:0000313|EMBL:ARV15118.1, ECO:0000313|Proteomes:UP000195470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-12 {ECO:0000313|EMBL:ARV15118.1,
RC ECO:0000313|Proteomes:UP000195470};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-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; CP019334; ARV15118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0MYE0; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000195470; 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}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000195470}.
FT DOMAIN 6..320
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 349 AA; 40093 MW; 5A99292BD0E0671B CRC64;
MKKKILITGG AGFIGSHVVR LFVNTYPEYD IFNLDSLTYA GNLENLSDID KSDNYTFLKG
DITNEEYIES IFKEYRFDSV VHLAAESHVD RSITDPLSFA KTNILGSMVL LNSFKNLWQN
NWNDKLFYHV STDEVYGTLG ETGLFTETTP YDPNSPYSAS KASSDHFVRA YGETYGLPYV
ISNCSNNYGA NQFPEKLIPL FINNIINNKA LPVYGNGKYT RDWLYVVDHA IAIDLVFHKG
KNKETYNIGG FNEWQNIDLI KLLCVQMNQK LGRSEGESEK LITYVKDRPG HDLRYAIDAS
KINKELGWKP SVTFEQGLSK TIDWYLNNKE WMQSIVNGDY KNYYEKQYK
//
