ID A0A410Q494_9FIRM Unreviewed; 342 AA.
AC A0A410Q494;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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 Name=rfbB {ECO:0000313|EMBL:QAT50103.1};
GN ORFNames=EQM14_10135 {ECO:0000313|EMBL:QAT50103.1};
OS Caproiciproducens sp. NJN-50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Caproiciproducens.
OX NCBI_TaxID=2507162 {ECO:0000313|EMBL:QAT50103.1, ECO:0000313|Proteomes:UP000287564};
RN [1] {ECO:0000313|EMBL:QAT50103.1, ECO:0000313|Proteomes:UP000287564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJN-50 {ECO:0000313|EMBL:QAT50103.1,
RC ECO:0000313|Proteomes:UP000287564};
RA Ma S.;
RT "Draft genomes of a novel of Caproiciproducens strains.";
RL Submitted (JAN-2019) 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; CP035283; QAT50103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410Q494; -.
DR KEGG; capr:EQM14_10135; -.
DR OrthoDB; 9811743at2; -.
DR Proteomes; UP000287564; 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, ECO:0000313|EMBL:QAT50103.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000287564}.
FT DOMAIN 5..308
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 342 AA; 38953 MW; B71AE80F781E285A CRC64;
MKIAVTGGAG FIGGNFIRYL LKNHPQDEVV CFDALTYAGN LESLGDILER PGFTFLRGDI
TNRSEVDSLF EKERPDILVN FAAESHVDRS IQNPGLFLQT NTVGTGILLD ACRKFGIERF
HQVSTDEVYG DLPLDRRDLF FTENTPINTS SPYSASKASA DLLAMAYHRT YQVPVTISRC
SNNYGPYQFP EKLIPLMIAN ALQELPLPVY GKGANIRDWL YVEDHCSAID LILRKGKAGE
IYNIGGHNER ANLQVVKAVL RELDKPESLI RFVTDRPGHD LRYAIDPTKI HRELGWLPTT
KFEDGIHTTI EWYLHHKTWR EHIATGEYRD YYEKWIETGD CR
//