ID   A0A145WIM6_9GAMM        Unreviewed;       351 AA.
AC   A0A145WIM6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=AMD27_00365 {ECO:0000313|EMBL:AMW77512.1};
OS   Acinetobacter sp. TGL-Y2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW77512.1, ECO:0000313|Proteomes:UP000076238};
RN   [1] {ECO:0000313|Proteomes:UP000076238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TGL-Y2 {ECO:0000313|Proteomes:UP000076238};
RA   Zhang G.;
RL   Submitted (APR-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; CP015110; AMW77512.1; -; Genomic_DNA.
DR   RefSeq; WP_067654817.1; NZ_CP015110.1.
DR   AlphaFoldDB; A0A145WIM6; -.
DR   STRING; 1407071.AMD27_00365; -.
DR   KEGG; acv:AMD27_00365; -.
DR   OrthoDB; 9803010at2; -.
DR   Proteomes; UP000076238; Chromosome.
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:UP000076238}.
FT   DOMAIN          4..324
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   351 AA;  39824 MW;  3BBF5FA614E2A28D CRC64;
     MKILVTGGAG FIGSAVVRHI IKNTENEVIN IDKLTYAGNL ESLAEIDQNE RYHFAQVDIC
     DAAALTQIFA TFAPDLVMHL AAESHVDRSI DGPSEFIQTN IVGTYTLLEV SRQYWQNLDE
     TKQQKFRFHH ISTDEVYGDL EGTTDLFTET TSYAPSSPYS ASKASSDHLV RAWHRTYGLP
     VIVTNCSNNY GPYHFPEKLI PLVILNALEA KPLPIYGKGD QIRDWLYVED HARALYKVVT
     EGVVGETYNI GGHNEKQNID VVKTICSILD ELRPQANNTP YASLITFVKD RPGHDLRYAI
     DASKMANELD WKPEESFETG IRKTVEWYLN NTQWVDHVKS GEYQNWLTKQ Y
//