ID A0A140L6V7_9CLOT Unreviewed; 336 AA.
AC A0A140L6V7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:KXG76282.1};
GN ORFNames=AN619_12390 {ECO:0000313|EMBL:KXG76282.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG76282.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG76282.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG76282.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-2015) 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:KXG76282.1}.
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DR EMBL; LOEE01000028; KXG76282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A140L6V7; -.
DR STRING; 520762.AN619_12390; -.
DR PATRIC; fig|520762.4.peg.1382; -.
DR OrthoDB; 9811743at2; -.
DR Proteomes; UP000070456; 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, ECO:0000313|EMBL:KXG76282.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000070456}.
FT DOMAIN 5..306
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 336 AA; 38229 MW; 50180CA6D75CF80E CRC64;
MKKLLVTGGA GFIGSNFIKY MLNKYKDYKI INLDLLTYAG NLENLQSVEC HPNYQFIRGS
IADKELVDKI VSDGIHYIIN FAAESHVDRS IENPGIFVET NIMGTQVLLD AAKKYGIEKY
IQISTDEVYG TLGSTGYFTE ETPLAPNSPY SASKASADLL ARAYHETFKL PVNITRCSNN
YGPYQFPEKL IPLMIANALE DKELPVYGDG LQIRDWLHVE DHCGAIDLVL HQGESGQVYN
IGGNNEKANI EIVKTILEKL GKPETLIKYV KDRPGHDRRY AIDSSKIQKE LGWKPQYTFE
AGIEKTIGWY LDHKVWWEKI RSGEYKVYYE KMYGNR
//
