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Database: UniProt
Entry: A0A1Y4TBG3_9FIRM
LinkDB: A0A1Y4TBG3_9FIRM
Original site: A0A1Y4TBG3_9FIRM 
ID   A0A1Y4TBG3_9FIRM        Unreviewed;       354 AA.
AC   A0A1Y4TBG3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=B5E66_06170 {ECO:0000313|EMBL:OUQ38582.1};
OS   Faecalibacterium sp. An121.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=1965550 {ECO:0000313|EMBL:OUQ38582.1, ECO:0000313|Proteomes:UP000196164};
RN   [1] {ECO:0000313|Proteomes:UP000196164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An121 {ECO:0000313|Proteomes:UP000196164};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-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:OUQ38582.1}.
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DR   EMBL; NFLM01000008; OUQ38582.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4TBG3; -.
DR   OrthoDB; 9811743at2; -.
DR   Proteomes; UP000196164; 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:UP000196164}.
FT   DOMAIN          5..321
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   354 AA;  40485 MW;  AF2DADBCAAFAAC71 CRC64;
     MKKYLITGCA GFIGSNFVYY MLKKHQDILL VNLDKLTYAG NLENLKGVEG DPRHVFVQGD
     ICDKELVEKL FAQYDFDYVI NFAAESHVDR SIANPEIFVQ TNVMGTVNLL QRAKEAWYDP
     AARTWKEGKK YLQVSTDEVY GALGAEGYFT ETTPLCPHSP YSSSKASADL FVMAFHDTYG
     MPVNITRCSN NYGPYQFPEK LIPLMINNVK HHKSLPVYGD GMQIRDWLYV EDHCKAIDMV
     ATGGKVGEVY NVGGHNERPN IFIVKTIISQ LHDRLQDEGI SEALIQHVAD RLGHDRRYGI
     DPAKIKNDLG WYPETPFEKG IVLTIDWYLS HQKWMDNVTS GSYQKYYEEM YKNK
//
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