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Database: UniProt
Entry: A0A370DA98_9GAMM
LinkDB: A0A370DA98_9GAMM
Original site: A0A370DA98_9GAMM 
ID   A0A370DA98_9GAMM        Unreviewed;       354 AA.
AC   A0A370DA98;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
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:RDH81217.1};
GN   ORFNames=DIZ80_14010 {ECO:0000313|EMBL:RDH81217.1};
OS   endosymbiont of Galathealinum brachiosum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=2200906 {ECO:0000313|EMBL:RDH81217.1, ECO:0000313|Proteomes:UP000254266};
RN   [1] {ECO:0000313|EMBL:RDH81217.1, ECO:0000313|Proteomes:UP000254266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1464 {ECO:0000313|EMBL:RDH81217.1};
RX   PubMed=30022157;
RA   Li Y., Liles M.R., Halanych K.M.;
RT   "Endosymbiont genomes yield clues of tubeworm success.";
RL   ISME J. 0:0-0(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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDH81217.1}.
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DR   EMBL; QFXC01000013; RDH81217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370DA98; -.
DR   Proteomes; UP000254266; 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:UP000254266}.
FT   DOMAIN          4..323
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   354 AA;  39840 MW;  4D4E5B1526CE9527 CRC64;
     MKIIVTGGAG FIGSAVIRQY TQETEHEVIN LDALTYAGNL ESLASVVEQP RYQFEHVDIK
     DINEVKRVFE RHKPDAVMHL AAESHVDRSI DAPADFIQTN IVGTLNLLEV ARKYWGELEG
     ARKDSFRFHH VSTDEVYGDL DETGLFTEET SYEPSSPYSA SKASSDHLVR AWHRTYGLPI
     VITNCSNNYG AFQFPEKLIP LITLNALEGK PLPIYGTGQQ IRDWLHVDDH ARALRLVLEK
     GANGQTYNIG GHNEKTNLQV VKTICSLLDK LVPDSPYIPH ESLITYVTDR PGHDLRYAID
     AGKIEKDLGW TPDETFETGI AKTIQWYLNN SEWCEHVQDG SYQGQRLGTG ENEE
//
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