ID   RMLC_MYCTO              Reviewed;         202 AA.
AC   P9WH10; L0TE75; O06330; Q7D5I3;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=dTDP-4-dehydrorhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P9WH11};
DE            EC=5.1.3.13 {ECO:0000250|UniProtKB:P9WH11};
DE   AltName: Full=Thymidine diphospho-4-keto-rhamnose 3,5-epimerase {ECO:0000250|UniProtKB:P9WH11};
DE   AltName: Full=dTDP-4-keto-6-deoxyglucose 3,5-epimerase {ECO:0000250|UniProtKB:P9WH11};
DE   AltName: Full=dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase {ECO:0000250|UniProtKB:P9WH11};
DE   AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P9WH11};
GN   Name=rmlC; Synonyms=strM; OrderedLocusNames=MT3571;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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       Involved in the biosynthesis of the dTDP-L-rhamnose which is a
CC       component of the critical linker, D-N-acetylglucosamine-L-rhamnose
CC       disaccharide, which connects the galactan region of arabinogalactan to
CC       peptidoglycan via a phosphodiester linkage.
CC       {ECO:0000250|UniProtKB:P9WH11}.
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:P9WH11};
CC   -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC       {ECO:0000250|UniProtKB:P26394}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WH11}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47911.1; -; Genomic_DNA.
DR   PIR; F70566; F70566.
DR   RefSeq; WP_003418610.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WH10; -.
DR   SMR; P9WH10; -.
DR   BindingDB; P9WH10; -.
DR   ChEMBL; CHEMBL4105851; -.
DR   EnsemblBacteria; AAK47911; AAK47911; MT3571.
DR   KEGG; mtc:MT3571; -.
DR   PATRIC; fig|83331.31.peg.3828; -.
DR   HOGENOM; CLU_090940_0_0_11; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019305; P:dTDP-rhamnose 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.
FT   CHAIN           1..202
FT                   /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT                   /id="PRO_0000428268"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   ACT_SITE        132
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         47..49
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HU21"
FT   SITE            138
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   202 AA;  22314 MW;  A6A1AFA0FC0F5871 CRC64;
     MKARELDVPG AWEITPTIHV DSRGLFFEWL TDHGFRAFAG HSLDVRQVNC SVSSAGVLRG
     LHFAQLPPSQ AKYVTCVSGS VFDVVVDIRE GSPTFGRWDS VLLDDQDRRT IYVSEGLAHG
     FLALQDNSTV MYLCSAEYNP QREHTICATD PTLAVDWPLV DGAAPSLSDR DAAAPSFEDV
     RASGLLPRWE QTQRFIGEMR GT