ID A0A1K2G0S9_9ACTN Unreviewed; 329 AA.
AC A0A1K2G0S9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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 Name=strE {ECO:0000313|EMBL:SFY53537.1};
GN ORFNames=STEPF1_06820 {ECO:0000313|EMBL:SFY53537.1};
OS Streptomyces sp. F-1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY53537.1, ECO:0000313|Proteomes:UP000095403};
RN [1] {ECO:0000313|EMBL:SFY53537.1, ECO:0000313|Proteomes:UP000095403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY53537.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FKJI03000043; SFY53537.1; -; Genomic_DNA.
DR RefSeq; WP_070026979.1; NZ_FKJI03000043.1.
DR AlphaFoldDB; A0A1K2G0S9; -.
DR OrthoDB; 9801785at2; -.
DR Proteomes; UP000095403; Unassembled WGS sequence.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 InterPro; IPR020904; Sc_DH/Rdtase_CS.
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.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU004473, ECO:0000313|EMBL:SFY53537.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000095403}.
FT DOMAIN 4..306
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 329 AA; 35686 MW; 3C09523EFF31224C CRC64;
MRLLVTGGAG FIGSEFVRSL LSSPDPVHRG LRITVLDDLT YAGVMANLAP VAGHPGFTFV
RGDICDADLV DQVLPGHDAV VHFAAESHVD RSIAGARPFA VTNVLGTQTL LDAAHRHGTG
RFVHVSTDEV YGSIDSGAWT EESPLAPNSP YAASKAGSDL LVLAAHRTHG LDVVVTRCSN
NYGPYQFPEK LIPLFVTNLL DGRHVPLYGA GRNVREWLHV VDHCRGIDLA LRKGRAGQVY
HLGGGRELTN SELTGLLLAA TGSGWEMVRR VPDRKGHDLR YALDCGKAEA ELGYTAEVEF
EDGLADTVAW YREHRDWWEP LKSAGPEAR
//
