ID A0A1I7JQM2_9FIRM Unreviewed; 361 AA.
AC A0A1I7JQM2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN02910342_02154 {ECO:0000313|EMBL:SFU87481.1};
OS Butyrivibrio sp. INlla21.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520811 {ECO:0000313|EMBL:SFU87481.1, ECO:0000313|Proteomes:UP000198910};
RN [1] {ECO:0000313|EMBL:SFU87481.1, ECO:0000313|Proteomes:UP000198910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INlla21 {ECO:0000313|EMBL:SFU87481.1,
RC ECO:0000313|Proteomes:UP000198910};
RA de Groot N.N.;
RL Submitted (OCT-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; FPCC01000017; SFU87481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7JQM2; -.
DR STRING; 1520811.SAMN02910342_02154; -.
DR Proteomes; UP000198910; 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..331
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 361 AA; 41689 MW; 55292070A20A290D CRC64;
MRTYLVTGGA GFIGSNYIHY MFKKYDNDIR IINVDVLTYA GNLENLRDVE NRDNYTFVRA
DITDREAIDK IFAENDIDRV VHFAAESHVD RSIVNPEIFV QTNVLGTATM LNAAKKAWEL
PDGSFKEGKK FLHVSTDEVY GTLDDDPNAY FYETTPYDPH SPYSASKAGS DMLVKAYMDT
YKFPANITNC SNNYGPYQFP EKLIPLVINN ALAGKDLPVY GDGKNVRDWL YVEDHAKAID
MVQEQGRLFE TYNVGGHNEK QNIEIVKTII DVLKEELDDS DPRKAHLSYD LIKYVTDRKG
HDRRYAIAPD KIKSEIGWEP ETMFKEGIRK TIKWYFENHE WMEHVTSGDY EKYYDAMYSN
K
//
