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Database: UniProt
Entry: A0A1H5VR35_9SPHI
LinkDB: A0A1H5VR35_9SPHI
Original site: A0A1H5VR35_9SPHI 
ID   A0A1H5VR35_9SPHI        Unreviewed;       351 AA.
AC   A0A1H5VR35;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN05421877_103209 {ECO:0000313|EMBL:SEF89769.1};
OS   Sphingobacterium lactis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=797291 {ECO:0000313|EMBL:SEF89769.1, ECO:0000313|Proteomes:UP000236731};
RN   [1] {ECO:0000313|Proteomes:UP000236731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22361 {ECO:0000313|Proteomes:UP000236731};
RA   Varghese N., Submissions S.;
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; FNUT01000003; SEF89769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5VR35; -.
DR   OrthoDB; 9801785at2; -.
DR   Proteomes; UP000236731; 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          6..320
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   351 AA;  39591 MW;  D282E1B5B3F08316 CRC64;
     MNKTILITGG AGFIGSHVVR TFVNKYPDYH IVNLDALTYA GNLENLRDVE NAANYTFCKA
     DIRDMDSMQQ VFSEFKPDAV IHLAAESHVD RSITDPMAFV NTNVIGTVNL LNAAKELWGA
     DFAGKRFHHV STDEVFGALG DTGFFTEETK YDPHSPYSAS KAASDHFVRA YHDTYGLPIV
     LTNCSNNYGP NHFPEKLIPL CILNILNNKP LPIYGDGKYT RDWLFVIDHA RAIDTVFHEG
     VNGQSYNVGG FNEWKNIDLV RELCKQMDEK LGREAGTSEQ LIQFVKDRPG HDLRYAIDAS
     KIKAELGWEP SVTFEQGLSK TIDWFLNNQE WLEQVSSGDY RKYYANHYGA V
//
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