ID   H3K9V3_9FIRM            Unreviewed;       339 AA.
AC   H3K9V3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=HMPREF9454_02026 {ECO:0000313|EMBL:EHR34520.1};
OS   Megamonas funiformis YIT 11815.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Megamonas.
OX   NCBI_TaxID=742816 {ECO:0000313|EMBL:EHR34520.1, ECO:0000313|Proteomes:UP000005963};
RN   [1] {ECO:0000313|EMBL:EHR34520.1, ECO:0000313|Proteomes:UP000005963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11815 {ECO:0000313|EMBL:EHR34520.1,
RC   ECO:0000313|Proteomes:UP000005963};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Megamonas funiformis YIT 11815.";
RL   Submitted (JAN-2012) 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:EHR34520.1}.
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DR   EMBL; ADMB01000088; EHR34520.1; -; Genomic_DNA.
DR   RefSeq; WP_008539586.1; NZ_JH601092.1.
DR   AlphaFoldDB; H3K9V3; -.
DR   STRING; 437897.GCA_900128435_00940; -.
DR   PATRIC; fig|742816.3.peg.1964; -.
DR   HOGENOM; CLU_007383_1_14_9; -.
DR   OrthoDB; 9766450at2; -.
DR   Proteomes; UP000005963; 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          4..309
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   339 AA;  38865 MW;  35E6975091B93ECD CRC64;
     MKILVTGGAG FIGSNFVYYE LDNYPNDEVI CLDKLTYAGN LETLEIAMKN PKFKFVKGDI
     ADRAFIDDLF ASEKPDVVVN FAAESHVDRS IENPEIFLQT NVIGTSVLMD ACHKYGNIRY
     HQVSTDEVYG DLPLDRPDLF FTETTPLHTS SPYSASKASA DLLVQAYYRT YKLPVTISRC
     SNNYGPYHFP EKLIPLMIAN ALNDKKLPVY GKGENVRDWL YVEDHCSAID LIIRKGKIGE
     VYNIGGHNER TNLEVVKTII KELGKSEDLI EFVTDRPGHD RRYAIDPTKI HNELGWLPAT
     KFDDGIKKTI DWYLTHKSWW EKIISGEYKD YYDKMYKNR
//