ID A0A2H9VT59_9SPHI Unreviewed; 350 AA.
AC A0A2H9VT59;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=CLV57_1003 {ECO:0000313|EMBL:PJJ84005.1};
OS Mucilaginibacter auburnensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1457233 {ECO:0000313|EMBL:PJJ84005.1, ECO:0000313|Proteomes:UP000242687};
RN [1] {ECO:0000313|EMBL:PJJ84005.1, ECO:0000313|Proteomes:UP000242687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28175 {ECO:0000313|EMBL:PJJ84005.1,
RC ECO:0000313|Proteomes:UP000242687};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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:PJJ84005.1}.
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DR EMBL; PGFJ01000001; PJJ84005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9VT59; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000242687; 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:UP000242687}.
FT DOMAIN 5..320
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 350 AA; 39602 MW; 24BBAADFD2A06902 CRC64;
MKKIIITGGA GFIGSHVVRR FVKNYPQYSI INLDKLTYAG NLANLKDIEN EPNYKFVKGD
IVDIAFINEL FETEKPDAVI HLAAESHVDR SIANPAEFVM TNVVGTVNLL TAARETWKGN
YDKTRFYHVS TDEVYGSLGE DGMFTEETAY DPHSPYSASK AGSDHFVRAY HDTYGIDTVI
SNCSNNYGSY HFPEKLIPLA INNIKNSKPV PVYGKGENIR DWLWVEDHAR AIDVIFHNAK
PGTTYNVGGH NEWKNIDLIK LLCSIMDKKL GREPGTSAKL ITFVTDRAGH DLRYAIDATK
LKNELGWVPG ITFEEGLEKT VDWYLENEGW LNDITSGHYQ QYYADQYNNR
//
