ID A0A1G7D5V8_9FLAO Unreviewed; 359 AA.
AC A0A1G7D5V8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05421544_11023 {ECO:0000313|EMBL:SDE46911.1};
OS Riemerella columbipharyngis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=1071918 {ECO:0000313|EMBL:SDE46911.1, ECO:0000313|Proteomes:UP000198517};
RN [1] {ECO:0000313|EMBL:SDE46911.1, ECO:0000313|Proteomes:UP000198517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24015 {ECO:0000313|EMBL:SDE46911.1,
RC ECO:0000313|Proteomes:UP000198517};
RA de Groot N.N.;
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; FNAS01000010; SDE46911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7D5V8; -.
DR STRING; 1071918.SAMN05421544_11023; -.
DR OrthoDB; 8967463at2; -.
DR Proteomes; UP000198517; 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}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000198517}.
FT DOMAIN 5..331
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 359 AA; 41070 MW; B1EE1F3D04886DDF CRC64;
MKSIIITGGA GFIGSHVVRE FVKYLPKTKI INLDALTYAG NLENLKDIEN EPNYIFEKAD
ITNTEELRAI FEKYCPDAVV HLAAESHVDR SITDPNAFIN TNVIGTANLL NLCKEFWTLN
PEHTHGNFPD EERQNLFYHV STDEVYGALG ETGFFTEETP YDPKSPYSAS KAASDHLVRA
YGNTYGLPYI ISNCSNNYGP NHFPEKLIPL CIFNIINEKP LPIYGDGKYT RDWLFVVDHA
KAIFKIFHEA KTGETYNIGG WNEWQNIDLI KELIKQMDAR LGRPEGYSER LITFVKDRPG
HDKRYAIDAT KLNKDLGWKP SVTFEQGLAK TIDWFLENKA WLEHVTSGAY QEYYSKQYK
//
