ID S9QSU1_9RHOB Unreviewed; 371 AA.
AC S9QSU1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=ruthe_03184 {ECO:0000313|EMBL:EPX82723.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX82723.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX82723.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX82723.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(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:EPX82723.1}.
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DR EMBL; AOLV01000039; EPX82723.1; -; Genomic_DNA.
DR AlphaFoldDB; S9QSU1; -.
DR STRING; 1123069.ruthe_03184; -.
DR PATRIC; fig|1123069.3.peg.3153; -.
DR HOGENOM; CLU_007383_1_14_5; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000015346; 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:EPX82723.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000015346}.
FT DOMAIN 4..318
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 371 AA; 41181 MW; 6E00B72EDDB7481E CRC64;
MRILVTGGAG FIGSAVVRRA VAMGHAVVNL DALTYAANPA NLAEVAASPL YAFEQADIRD
RVALDRIFRD HRPDAVMHLA AESHVDRSID GPAAFVETNV TGTFHLLEAA RAHWLREGRP
PGFRFHHIST DEVFGSLGPE GRFTEETRYD PRSPYSASKA ASDHLVRAWG ETYGLPVLVT
NCSNNYGPYH FPEKLVPVTI LNALHGRPIP VYGTGENVRD WLYVEDHAEA LLLVLERGAV
GRTYAIGGES EARNIDLVRM ICSIMDEMHP AGAPHDRLIT FVPDRPGHDL RYAIDPSRIR
AELGWRPSVT LQEGLRRTVR WYLDREDWWR PLLGRDGWGG GWGPGHEDPG SSAGPDRWHR
RCAAARRPGC S
//
