ID   A0A385C9N9_9GAMM        Unreviewed;       356 AA.
AC   A0A385C9N9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   Name=rfbB {ECO:0000313|EMBL:AXQ23915.1};
GN   ORFNames=BEN71_18465 {ECO:0000313|EMBL:AXQ23915.1};
OS   Acinetobacter wuhouensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1879050 {ECO:0000313|EMBL:AXQ23915.1, ECO:0000313|Proteomes:UP000257257};
RN   [1] {ECO:0000313|EMBL:AXQ23915.1, ECO:0000313|Proteomes:UP000257257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHA60 {ECO:0000313|EMBL:AXQ23915.1,
RC   ECO:0000313|Proteomes:UP000257257};
RX   PubMed=30117799; DOI=10.1099/ijsem.0.002963;
RA   Hu Y., Feng Y., Qin J., Radolfova-Krizova L., Maixnerova M., Zhang X.,
RA   Nemec A., Zong Z.;
RT   "Acinetobacter wuhouensis sp. nov., isolated from hospital sewage.";
RL   Int. J. Syst. Evol. Microbiol. 68:3212-3216(2018).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP031716; AXQ23915.1; -; Genomic_DNA.
DR   RefSeq; WP_068975564.1; NZ_CP031716.1.
DR   AlphaFoldDB; A0A385C9N9; -.
DR   STRING; 1879050.GCA_001696605_02765; -.
DR   KEGG; awu:BEN71_18465; -.
DR   OrthoDB; 9803010at2; -.
DR   Proteomes; UP000257257; 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, ECO:0000313|EMBL:AXQ23915.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          4..324
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   356 AA;  40501 MW;  47E42B25116478FE CRC64;
     MKVLVTGGAG FIGSAVVRHI IKNTQDEVLN IDKLTYAGNL ESLKDVEQNE KYQFKQIDIC
     NANELTVAFN EFEPDLVMHL AAESHVDRSI DGPAEFIATN IVGTYTLLEV ARKYWMQLDE
     QAKTKFKFHH ISTDEVYGDL EGTTDLFTET TSYAPSSPYS ASKASSDHLV RAWQRTYGLP
     TIVTNCSNNY GPYHFPEKLI PLVILNALDG KPLPIYGKGD QIRDWLFVED HARALYKVVT
     EGVVGETYNI GGHNEKQNID VVKTICKILD ELRPQANQQS YESLITFVKD RPGHDLRYAI
     DATKISNDLG WKPEETFDTG IRKTVEWYLN NQDWVVHVQS GEYQNWVQQQ YENRLA
//