ID   RMLC_NEIGO              Reviewed;         328 AA.
AC   P37763;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=dTDP-4-dehydrorhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE            EC=5.1.3.13 {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=Thymidine diphospho-4-keto-rhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=dTDP-4-keto-6-deoxyglucose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase {ECO:0000250|UniProtKB:P26394};
DE   AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P26394};
GN   Name=rfbC; Synonyms=rmlC;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=7961452; DOI=10.1128/jb.176.22.6915-6920.1994;
RA   Robertson B.D., Frosch M., van Putten J.P.M.;
RT   "The identification of cryptic rhamnose biosynthesis genes in Neisseria
RT   gonorrhoeae and their relationship to lipopolysaccharide biosynthesis.";
RL   J. Bacteriol. 176:6915-6920(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=8655518; DOI=10.1128/jb.178.11.3342-3345.1996;
RA   Petering H., Hammerschmidt S., Frosch M., van Putten J.P.M., Ison C.A.,
RA   Robertson B.D.;
RT   "Genes associated with meningococcal capsule complex are also found in
RT   Neisseria gonorrhoeae.";
RL   J. Bacteriol. 178:3342-3345(1996).
CC   -!- FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of
CC       dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-
CC         L-rhamnose; Xref=Rhea:RHEA:16969, ChEBI:CHEBI:57649,
CC         ChEBI:CHEBI:62830; EC=5.1.3.13;
CC         Evidence={ECO:0000250|UniProtKB:P26394};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000250|UniProtKB:P26394}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26394}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; Z32742; CAA83654.1; -; Genomic_DNA.
DR   EMBL; Z21508; CAA79720.1; -; Genomic_DNA.
DR   PIR; S47047; S47047.
DR   AlphaFoldDB; P37763; -.
DR   SMR; P37763; -.
DR   UniPathway; UPA00124; -.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase 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   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR000888; dTDP_sugar_isom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR21047; PTHR21047; 1.
DR   Pfam; PF00908; dTDP_sugar_isom; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   TIGRFAMs; TIGR01221; rmlC; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Lipopolysaccharide biosynthesis.
FT   CHAIN           1..328
FT                   /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT                   /id="PRO_0000207981"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         46..48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         58
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   SITE            136
FT                   /note="Participates in a stacking interaction with the
FT                   thymidine ring of dTDP-4-oxo-6-deoxyglucose"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SFD1"
SQ   SEQUENCE   328 AA;  37209 MW;  20BA7BA065604D4F CRC64;
     MDIIDTALPD VKLLKPQVFT DGRGFFMETF RDGWFKENIA DRTFVQENHS NSSKGVLRGL
     HYQTENTQGK LVRVVVGEVF DVAVDMREGS PTFGKWAGAT LSAQNRYQLW IPEGFAHGFC
     VLGDAAEVVY KCTDYYNPET EQVLIWNDPA IGIGWPLQTA PLLSPKDLAG KTWAQAEKSA
     LRFPDKKCRP NVSDGIFSDR LPTRLQYALC KEKHPGNEER QAQPRSGGIP VLQIQRERRI
     RAAVGHREGN NKRHNYTNQA FTDNQACREK RTDTVGVFQT AFAVFRLLAN DVFQHRRQHR
     ACHDGHIDGR RQINAHTDRK DGQGKFTA