ID A0A495JLD9_9ACTN Unreviewed; 362 AA.
AC A0A495JLD9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00016977, ECO:0000256|RuleBase:RU004473};
DE EC=4.2.1.46 {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
GN ORFNames=BDK92_3813 {ECO:0000313|EMBL:RKR89465.1};
OS Micromonospora pisi.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=589240 {ECO:0000313|EMBL:RKR89465.1, ECO:0000313|Proteomes:UP000277671};
RN [1] {ECO:0000313|EMBL:RKR89465.1, ECO:0000313|Proteomes:UP000277671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45175 {ECO:0000313|EMBL:RKR89465.1,
RC ECO:0000313|Proteomes:UP000277671};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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:RKR89465.1}.
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DR EMBL; RBKT01000001; RKR89465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495JLD9; -.
DR Proteomes; UP000277671; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000277671}.
FT DOMAIN 36..333
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 362 AA; 40613 MW; C399747272F42B9E CRC64;
MPAPPDSAAI PTRSTGDSAR LCVILGAVTM APMRLLVTGG AGFIGSNFVR QALDALDCQV
DVLDALTYAG DRSSLAEVEH RINFVHGSVT DAAIVDELVR QADTVVHFAA ESHNDNSVVD
PSPFVQTNLI GTFNILESVR RHDKRLHHIS TDEVFGDLEL DEERRFTEES AFDPSSPYSS
TKAGSDLMVR GWIRSFGVRA TISHCSNNYG PFHHIEKFIP RQITNVIDGV RPKVYGSGQN
VRDWIHVHDH NTAVNAILER GRIGQTYLIG AECELNNIVV VQEILRLMGR PDDWFDMVGD
RPGHDLRYAI DSSKLQAELG WKPQYLNFRD GLAQTIEWYQ QNESWWRPKK EATEAKYREM
GR
//
