ID A0A434AUG4_9BACT Unreviewed; 351 AA.
AC A0A434AUG4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 08-NOV-2023, entry version 10.
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:RUT77984.1};
GN ORFNames=DLK05_10050 {ECO:0000313|EMBL:RUT77984.1};
OS Ancylomarina longa.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2487017 {ECO:0000313|EMBL:RUT77984.1, ECO:0000313|Proteomes:UP000282985};
RN [1] {ECO:0000313|EMBL:RUT77984.1, ECO:0000313|Proteomes:UP000282985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3-2 S1-C {ECO:0000313|EMBL:RUT77984.1,
RC ECO:0000313|Proteomes:UP000282985};
RA Fu T.;
RT "Parancylomarina longa gen. nov., sp. nov., isolated from sediments of
RT southern Okinawa.";
RL Submitted (NOV-2018) 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:RUT77984.1}.
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DR EMBL; RJJX01000012; RUT77984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A434AUG4; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000282985; 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:RUT77984.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000282985}.
FT DOMAIN 6..321
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 351 AA; 39871 MW; 2F75A2025E270697 CRC64;
MKKKILITGG AGFIGSHVVR LFVNKYPNYQ IVNLDALTYA GNLENLNDID SNANYSFIKG
DITDLTFVTD LFQKHQFDGV LHLAAESHVD RSISDPLAFI TTNIVGTVNL LNAAKETWKN
NMEGKMFYHI STDEVYGSLG KEGKFTETTP YDPRSPYSAS KASSDHLVRA YHHTYNLPVV
LSNCSNNYGA NQFPEKLIPL VINNIKNSKP LPIYGKGENV RDWLFVEDHA LAIDLIYHQG
KIGETYNIGG NNEWSNLALV KKLCDIMDLK LGQELGTAQK LITFVKDRAG HDLRYAIDAT
KIEKELGWNP SIKFEEGFEK TIDWYLSHSE WLDHILSGDY EKYYNQQYEK R
//
