ID A0A1H9BWZ5_9GAMM Unreviewed; 363 AA.
AC A0A1H9BWZ5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=SAMN04488038_102259 {ECO:0000313|EMBL:SEP93409.1};
OS Solimonas aquatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Solimonas.
OX NCBI_TaxID=489703 {ECO:0000313|EMBL:SEP93409.1, ECO:0000313|Proteomes:UP000199233};
RN [1] {ECO:0000313|EMBL:SEP93409.1, ECO:0000313|Proteomes:UP000199233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25927 {ECO:0000313|EMBL:SEP93409.1,
RC ECO:0000313|Proteomes:UP000199233};
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; FOFS01000002; SEP93409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9BWZ5; -.
DR STRING; 489703.SAMN04488038_102259; -.
DR Proteomes; UP000199233; 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; 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}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000199233}.
FT DOMAIN 9..334
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 363 AA; 40888 MW; CCAC227E64F5A92F CRC64;
MSYQAQNMLV TGGAGFIGSN FVRYLLGADA SVRIVNLDLL TYAGKLENLE DLPGADRHHF
VKGDICDREL IDKLLREHRI DTVVHFAAES HVDRSIHGPG EFVRTNVVGT FTLLESARQY
WMAEQKLDKA ALAAQRRFHH ISTDEVYGSL GPQDPPFRET NPYEPNSPYS ASKAGSDHLV
RAYFHTYGFP VTTTNCSNNY GPYHFPEKLI PLIILNALQG KPLPVYGDGQ NVRDWLFVTD
HASAIARVLQ AGKTGETYNV GGWNEKKNLD VVEQICAILD ELSPRKDGKR YGEQIRFVTD
RPGHDRRYAI DAGKLERELG WKPAETFETG IRKTVRWYLD NLIWAEKVTG SAYGDWIAKQ
YGA
//