ID A0A1H1L645_9ACTO Unreviewed; 335 AA.
AC A0A1H1L645;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00016977, ECO:0000256|RuleBase:RU004473};
DE EC=4.2.1.46 {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
GN ORFNames=SAMN04489715_0831 {ECO:0000313|EMBL:SDR70051.1};
OS Schaalia meyeri.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=52773 {ECO:0000313|EMBL:SDR70051.1, ECO:0000313|Proteomes:UP000181914};
RN [1] {ECO:0000313|Proteomes:UP000181914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20733 {ECO:0000313|Proteomes:UP000181914};
RA Varghese 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; FNLK01000008; SDR70051.1; -; Genomic_DNA.
DR RefSeq; WP_050695094.1; NZ_FNLK01000008.1.
DR AlphaFoldDB; A0A1H1L645; -.
DR STRING; 52773.ADJ76_05275; -.
DR KEGG; amy:ADJ76_05275; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000181914; 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}.
FT DOMAIN 5..307
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 335 AA; 37187 MW; 920EC52D69CCA7EA CRC64;
MKIVVTGGAG FIGANFVHTL LEDHPDVDVV VLDKFTYAGN RASLADIPED QAPRLTVVEG
DVTDADLVDG LVAGADAVVH FAAESHNDNS LLDPSPFIQT NLVGTFTLLE AVRRHKVRFH
HISTDEVYGD LELDDPAKFT PTTPYNPSSP YSSSKAGSDL LVRAWVRSFG VEATISNCSN
NYGPYQHIEK FIPRMITNRL RGVRPRLYGD GLNVRDWIHV RDHNTAVWDI LMRGRIGDTY
LIGADGETNN RDVVAILNEL MGFAPDDFDH VSDRPGHDLR YAIDNSKLVT ELGWQPRFTN
FRDGLADTIA WYTGNEAWWA PLKEAVEAKY AAEGH
//
