ID   WBIB_BURTA              Reviewed;         363 AA.
AC   Q2SYH7;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=dTDP-L-rhamnose 4-epimerase;
DE            EC=5.1.3.25;
GN   Name=wbiB; OrderedLocusNames=BTH_I1476;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=21640586; DOI=10.1016/j.bmcl.2011.05.030;
RA   Yoo H.G., Kwon S.Y., Karki S., Kwon H.J.;
RT   "A new route to dTDP-6-deoxy-l-talose and dTDP-L-rhamnose: dTDP-L-rhamnose
RT   4-epimerase in Burkholderia thailandensis.";
RL   Bioorg. Med. Chem. Lett. 21:3914-3917(2011).
CC   -!- FUNCTION: Catalyzes the interconvertion of dTDP-6-deoxy-L-talose and
CC       dTDP-L-rhamnose. The equilibrium is strongly toward dTDP-L-rhamnose.
CC       {ECO:0000269|PubMed:21640586}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-6-deoxy-beta-L-talose = dTDP-beta-L-rhamnose;
CC         Xref=Rhea:RHEA:34451, ChEBI:CHEBI:57510, ChEBI:CHEBI:68576;
CC         EC=5.1.3.25; Evidence={ECO:0000269|PubMed:21640586};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=24.7 uM for dTDP-6-deoxy-L-talose {ECO:0000269|PubMed:21640586};
CC         Note=kcat is 0.9 sec(-1) for dTDP-6-deoxy-L-talose.;
CC       pH dependence:
CC         Optimum pH is 7.8-8.4. {ECO:0000269|PubMed:21640586};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000269|PubMed:21640586}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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; CP000086; ABC37367.1; -; Genomic_DNA.
DR   RefSeq; WP_009889595.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SYH7; -.
DR   SMR; Q2SYH7; -.
DR   PRIDE; Q2SYH7; -.
DR   EnsemblBacteria; ABC37367; ABC37367; BTH_I1476.
DR   KEGG; bte:BTH_I1476; -.
DR   HOGENOM; CLU_007383_1_7_4; -.
DR   OMA; GPRMPRD; -.
DR   OrthoDB; 1180629at2; -.
DR   BRENDA; 5.1.3.25; 8156.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000001930; Chromosome I.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Lipopolysaccharide biosynthesis; NAD.
FT   CHAIN           1..363
FT                   /note="dTDP-L-rhamnose 4-epimerase"
FT                   /id="PRO_0000424103"
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         18..24
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         68..69
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         90..94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  39159 MW;  831CF0462F3AAD32 CRC64;
     MSDVNASLVD GKKILVTGGA GFIGCAISER LAARASRYVV MDNLHPQIHA NAVRPVALHE
     KAELVVADVT DAGAWDALLS DFQPEIIIHL AAETGTGQSL TEASRHALVN VVGTTRLTDA
     IVKHGIAVEH ILLTSSRAVY GEGAWQKADG TIVYPGQRGR AQLEAAQWDF PGMTMLPSRA
     DRTEPRPTSV YGATKLAQEH VLRAWSLATK TPLSILRLQN VYGPGQSLTN SYTGIVALFS
     RLAREKKVIP LYEDGNVTRD FVSIDDVADA IVATLAREPE ALSLFDIGSG QATSILDMAR
     IIAAHYGAPE PQVNGAFRDG DVRHAACDLS ESLANLGWKP QWSLERGIGE LQTWIAQELD
     RKN