ID A0A0N1NNQ0_9ACTN Unreviewed; 359 AA.
AC A0A0N1NNQ0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00016977, ECO:0000256|RuleBase:RU004473};
DE EC=4.2.1.46 {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
GN ORFNames=OK074_7190 {ECO:0000313|EMBL:KPI22402.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI22402.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI22402.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI22402.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) 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:KPI22402.1}.
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DR EMBL; LJCV01000021; KPI22402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NNQ0; -.
DR PATRIC; fig|1592327.3.peg.849; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000037991; 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, ECO:0000313|EMBL:KPI22402.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991}.
FT DOMAIN 68..342
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 38586 MW; 4EB6B56080890BE5 CRC64;
MTEPRTTSAA PSPSVSGSAP AGARVLVTGG AGFIGSHYVR TLLGASGPGG PGGPGDPGGP
GGPFSGSVTV LDKLTYAGNP ANLDPVRDHP GFAFVQGDIC DGEFVDDLMA RHDDVVHFAA
ESHVDRSILS SGEFVRTNVL GTQTLLDAAL RHGIRTFVHV STDEVYGSID TGAWTEQSPL
LPNSPYSAAK ASSDLLALAH HRTHGLDVRV TRCSNNYGHH QHPEKVVPLF VTNLLDGLTV
PLYGDGGNVR DWLHIDDHVQ GIELVRTGGR AGEVYNIGGG TELTNRQLTE LLLEACGAGP
DRIEYVPDRK GHDRRYCVDW TKIRDELGYR PRKDFAAGLA ETVEWYRENR GWWEPLKKG
//
