TGDS_BOVIN
ID TGDS_BOVIN Reviewed; 355 AA.
AC A6QLW2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=dTDP-D-glucose 4,6-dehydratase;
DE EC=4.2.1.46;
GN Name=TGDS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) 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 -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}.
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DR EMBL; BC148106; AAI48107.1; -; mRNA.
DR RefSeq; NP_001094629.1; NM_001101159.1.
DR AlphaFoldDB; A6QLW2; -.
DR SMR; A6QLW2; -.
DR STRING; 9913.ENSBTAP00000006984; -.
DR PaxDb; A6QLW2; -.
DR PRIDE; A6QLW2; -.
DR GeneID; 534594; -.
DR KEGG; bta:534594; -.
DR CTD; 23483; -.
DR eggNOG; KOG0747; Eukaryota.
DR HOGENOM; CLU_007383_1_14_1; -.
DR InParanoid; A6QLW2; -.
DR OrthoDB; 815803at2759; -.
DR TreeFam; TF313892; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IBA:GO_Central.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Lyase; NAD; Reference proteome.
FT CHAIN 1..355
FT /note="dTDP-D-glucose 4,6-dehydratase"
FT /id="PRO_0000328213"
FT ACT_SITE 143
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 40666 MW; 871C965B58BEF68C CRC64;
MSVAGRAESL GPPDSFAKRV LVTGGAGFIA SHMIVSLVED YPNYMIINLD KLDYCASLKN
LETISNKQNY KFIQGDICDS HFVKLLFETE KIDIVLHFAA QTHVDLSFVR AFEFTYVNVY
GTHVLVSAAH EARVEKFIYV STDEVYGGSL DKEFDESSPK QPTNPYASSK AAAECFVQSY
WEQYKFPVVI TRSSNVYGPH QYPEKVIPKF ISLLQHNRKC CIHGTGLQTR NFLYATDVVE
AFLTVLKKGK PGEIYNIGTN FEMSVLQLAK ELIQLIKETN SESEMENWVD YVDDRPTNDM
RYPMKSEKIH GLGWRPKVPW KEGIKKTIEW YRENFHNWKN AEKALEPFPV QPPFV