ID A0A411WFU3_9GAMM Unreviewed; 355 AA.
AC A0A411WFU3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 Name=rffG {ECO:0000313|EMBL:QBH95105.1};
GN ORFNames=EKN56_00940 {ECO:0000313|EMBL:QBH95105.1};
OS Limnobaculum zhutongyuii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Limnobaculum.
OX NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH95105.1, ECO:0000313|Proteomes:UP000293154};
RN [1] {ECO:0000313|EMBL:QBH95105.1, ECO:0000313|Proteomes:UP000293154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF-458 {ECO:0000313|EMBL:QBH95105.1,
RC ECO:0000313|Proteomes:UP000293154};
RA Ge Y.;
RT "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL Submitted (MAR-2019) 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; CP034752; QBH95105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WFU3; -.
DR KEGG; prag:EKN56_00940; -.
DR OrthoDB; 9803010at2; -.
DR Proteomes; UP000293154; Chromosome.
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; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR43000:SF47; DTDP-GLUCOSE 4,6-DEHYDRATASE 2; 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, ECO:0000313|EMBL:QBH95105.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027}.
FT DOMAIN 5..327
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 355 AA; 39985 MW; 5879B8366A9DD834 CRC64;
MRKILVTGGA GFIGSAVVRH IIQDTKDSVL VVDKLTYAGN LDSLVEVSDS GRYSFEQVDI
CDRSALDRLF TQYQPDLVMH LAAESHVDRS IDGPAAFIET NIVGTYTLLE AARHYWMGLD
TALKQAFRFH HISTDEVYGD LHGTTDLFTE TTPYAPSSPY SASKASSDHL VRAWLRTYGF
PTIVTNCSNN YGPYHFPEKL IPLIILNALE GKALPVYGNG AQVRDWLFVE DHARALYKVV
TEGVVGETYN IGGHNERKNI EVVRTICQLL EELAPSKPDG VAKYEDLITY VTDRPGHDMR
YAIDASKIER ELNWKPLETF ESGIRKTVSW YLTNQAWWQR VQDGSYARER IGLKS
//
