ID A0A1I2TRB7_9SPHI Unreviewed; 350 AA.
AC A0A1I2TRB7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN04489864_101549 {ECO:0000313|EMBL:SFG67450.1};
OS Pedobacter insulae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=414048 {ECO:0000313|EMBL:SFG67450.1, ECO:0000313|Proteomes:UP000199666};
RN [1] {ECO:0000313|EMBL:SFG67450.1, ECO:0000313|Proteomes:UP000199666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18684 {ECO:0000313|EMBL:SFG67450.1,
RC ECO:0000313|Proteomes:UP000199666};
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; FOPP01000001; SFG67450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2TRB7; -.
DR STRING; 414048.SAMN04489864_101549; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000199666; 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:UP000199666}.
FT DOMAIN 5..320
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 350 AA; 39891 MW; 2C97EDD27E54CE13 CRC64;
MKKILITGGA GFIGSHVVRR FLINYPQYEV VNLDALTYAG NLANLKDVEN LPNYRFLKAD
ITDAKLISQI FQAENFDAVI HLAAESHVDR SIADPNAFVI TNVLGTVNLL NAAREYWKGS
YHEKRFYHVS TDEVYGALGD EGMFTETTAY DPHSPYSASK ASSDHFVRAY HDTYGMDCVI
SNCSNNYGSH HFPEKLIPLA INNIKNNKPV PVYGKGENVR DWLWVEDHAR AIDVIFHGAK
SGETYNIGGH NEWKNIDLIR LLCEVMDEKL NREKGESAKL ITFVTDRAGH DLRYAIDSTK
LQNELNWVPS LQFEEGLAKT VDWYLANEEW LMNVTSGNYQ SYYETQYRER
//
