ID A0A1G9S625_9BURK Unreviewed; 353 AA.
AC A0A1G9S625;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05428957_104126 {ECO:0000313|EMBL:SDM30852.1};
OS Oryzisolibacter propanilivorax.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Oryzisolibacter.
OX NCBI_TaxID=1527607 {ECO:0000313|EMBL:SDM30852.1, ECO:0000313|Proteomes:UP000198552};
RN [1] {ECO:0000313|Proteomes:UP000198552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPL6 {ECO:0000313|Proteomes:UP000198552};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FNHP01000004; SDM30852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9S625; -.
DR STRING; 1527607.SAMN05428957_104126; -.
DR OrthoDB; 9803010at2; -.
DR Proteomes; UP000198552; Unassembled WGS sequence.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 InterPro; IPR020904; Sc_DH/Rdtase_CS.
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.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU004473}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000198552}.
FT DOMAIN 3..323
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 353 AA; 39980 MW; B1318843D6A94CE0 CRC64;
MILVTGGAGF IGANFVLDWL AQCDEPVLNL DKLTYAGNVH NLDSLSQDTR HTFVQGDIAD
RTLLDRLLAQ HRPRAVVNFA AESHVDRSIH GPEDFIQTNV VGTFRLLEAV RQHWSGLPAM
EKEAFRFLHV STDEVYGTLE PEAPAFTETH NYEPNSPYSA SKAASDHLVR AWHHTYGLPV
LTTNCSNNYG PYHFPEKLIP LVIVNALAGK PLPIYGDGRQ IRDWLYVRDH CSAIRRVLEA
GRLGETYNVG GWNESANIDI VRLICSLLDE LRPRADGQSY AAQITHVTDR PGHDRRYAID
ARKLERELGW KPAETFETGI RKTVQWYLEH PEWVAQVQSG AYRDWVQKQY QSA
//
