ID A0A1F8AV48_9BACT Unreviewed; 334 AA.
AC A0A1F8AV48;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 08-NOV-2023, entry version 14.
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=A3E44_03795 {ECO:0000313|EMBL:OGM55379.1};
OS Candidatus Woesebacteria bacterium RIFCSPHIGHO2_12_FULL_41_24.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802510 {ECO:0000313|EMBL:OGM55379.1, ECO:0000313|Proteomes:UP000178603};
RN [1] {ECO:0000313|EMBL:OGM55379.1, ECO:0000313|Proteomes:UP000178603}
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:OGM55379.1}.
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DR EMBL; MGGW01000004; OGM55379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8AV48; -.
DR Proteomes; UP000178603; 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..305
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 334 AA; 38296 MW; 6483144D41CB6F73 CRC64;
MRLLVTGGCG FIGSNFICYW LKKYHGDKVL NLDKLTYAGH LSSTIDFDEN KNYSFVKGDI
CYPEIVAKCM KNVDIVVHFA AESHVDRSIT DPTIFSRTNV LGTQVLLDAA LRVKVKRFHH
VSTDEVFGDL PLNSKHKFRE DTLYNPHSPY AASKAASDHL VRAYHYTFGL PVTITNGANN
YGPCQDPEKF MPRAITNLIE NTPIKLYGKG DNIRNWLYVE DYCSAIDLVI TKGKIGETYL
VGGSSKELTN YDVARLIVGF FGLDKKYIKF VKDRSGHDRK YAIDSTKLKT LGWQPKYDFD
KWLSKTIDWY KKNTWWWRPL KAKAENLYRK TGQI
//
