ID A0A1F8SVT9_9CHLR Unreviewed; 334 AA.
AC A0A1F8SVT9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 15.
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};
DE Flags: Fragment;
GN ORFNames=A2029_03735 {ECO:0000313|EMBL:OGO64035.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_47_9.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797665 {ECO:0000313|EMBL:OGO64035.1, ECO:0000313|Proteomes:UP000178740};
RN [1] {ECO:0000313|EMBL:OGO64035.1, ECO:0000313|Proteomes:UP000178740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGO64035.1}.
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DR EMBL; MGOG01000116; OGO64035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SVT9; -.
DR Proteomes; UP000178740; 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..326
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
FT NON_TER 334
FT /evidence="ECO:0000313|EMBL:OGO64035.1"
SQ SEQUENCE 334 AA; 37847 MW; C862EDBCCCDB5ED1 CRC64;
MRNVLVTGGA GFIGSNFIRF LLNVEPDVQV VNLDVLSYAG SFENLKNLPF PERHIFIKGD
ICDRSLVDQL FDAHKIDTVV HFAAETHVDR SIHSPEIFLR TNVEGTFTLL EAARRFWLSE
KILSTDDLRF HHISTDEVFG FLKPDDPAWT EDMPYAPSSP YSASKAASDH YVRSYGHTYG
LPYSITNCSN NYGPYQFPEK LIPLMILNAQ DGKTLPIYGD GGQIRDWLFV EDHCEAIWTV
LRKGRLGQTY NIGGGSQPTN LEIVQHLCAA MDELLPHSPF CPHSSLMRFV PDRPGHDRRY
AIDFTKIKTQ LGWQPKQSLG TGLQKTIEWY LSNP
//
