ID   RMLB_XANCB              Reviewed;         351 AA.
AC   B0RVL0; P55295;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000250|UniProtKB:P27830};
DE            EC=4.2.1.46 {ECO:0000250|UniProtKB:P27830};
GN   Name=rfbB; Synonyms=rmlB; OrderedLocusNames=xcc-b100_3734;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8253667; DOI=10.1128/jb.175.24.7786-7792.1993;
RA   Koeplin R., Wang G., Hoette B., Priefer U.B., Puehler A.;
RT   "A 3.9-kb DNA region of Xanthomonas campestris pv. campestris that is
RT   necessary for lipopolysaccharide production encodes a set of enzymes
RT   involved in the synthesis of dTDP-rhamnose.";
RL   J. Bacteriol. 175:7786-7792(1993).
RN   [2]
RP   SEQUENCE REVISION TO 8 AND 15.
RA   Vorholter F.J., Niehaus K., Puehler A.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
CC   -!- FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-
CC       deoxy-D-xylo-4-hexulose via a three-step process involving oxidation,
CC       dehydration and reduction. {ECO:0000250|UniProtKB:P27830}.
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:0000250|UniProtKB:P27830};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000250|UniProtKB:P27830};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000250|UniProtKB:P27830};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000250|UniProtKB:P37759}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000250|UniProtKB:P37759}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27830}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. dTDP-glucose dehydratase subfamily.
CC       {ECO:0000250|UniProtKB:P27830}.
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DR   EMBL; AF204145; AAK53466.1; -; Genomic_DNA.
DR   EMBL; AM920689; CAP53101.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RVL0; -.
DR   SMR; B0RVL0; -.
DR   PRIDE; B0RVL0; -.
DR   KEGG; xca:xcc-b100_3734; -.
DR   HOGENOM; CLU_007383_1_14_6; -.
DR   OMA; EWCQHVQ; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
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.
DR   TIGRFAMs; TIGR01181; dTDP_gluc_dehyt; 1.
PE   3: Inferred from homology;
KW   Lipopolysaccharide biosynthesis; Lyase; NAD.
FT   CHAIN           1..351
FT                   /note="dTDP-glucose 4,6-dehydratase"
FT                   /id="PRO_0000333184"
FT   ACT_SITE        134
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   ACT_SITE        135
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         12..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         32..35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         58..59
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         80..84
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
FT   BINDING         99
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
FT   BINDING         158..162
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
FT   BINDING         188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P27830"
FT   BINDING         197..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
FT   BINDING         213..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
FT   BINDING         289..293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P26391"
SQ   SEQUENCE   351 AA;  38558 MW;  F1B393B1A2EA0F3F CRC64;
     MATWLVTGGA GFIGGNFVLE AVSRGIRVVN LDALTYAGNL NTLASLEGNA DHIFVKGDIG
     DGALVTRLLQ EHQPDAVLNF AAESHVDRSI EGPGAFIQTN VVGTLALLEA VRDYWKALPD
     TRRDAFRFLH VSTDEVYGTL GETGKFTETT PYAPNSPYSA SKAASDHLVR AFHHTYGLPV
     LTTNCSNNYG PYHFPEKLIP LVIAKALAGE PLPVYGDGKQ VRDWLFVSDH CEAIRTVLAK
     GRVGETYNVG GNSERQNIEV VQAICALLDQ HRPREDGKPR ESQIAYVTDR PGHDRRYAID
     ASKLKDELGW EPAYTFEQGI ALTVDWYLTN QTWVQGVLDG SYRLERIGAT V