RMLC_ECOLI
ID RMLC_ECOLI Reviewed; 185 AA.
AC P37745;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 151.
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; OrderedLocusNames=b2038, JW2023;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7517390; DOI=10.1128/jb.176.13.4133-4143.1994;
RA Yao Z., Valvano M.A.;
RT "Genetic analysis of the O-specific lipopolysaccharide biosynthesis region
RT (rfb) of Escherichia coli K-12 W3110: identification of genes that confer
RT group 6 specificity to Shigella flexneri serotypes Y and 4a.";
RL J. Bacteriol. 176:4133-4143(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / WG1;
RX PubMed=7517391; DOI=10.1128/jb.176.13.4144-4156.1994;
RA Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M.,
RA Redmond J.W., Lindquist L., Reeves P.R.;
RT "Structure of the O antigen of Escherichia coli K-12 and the sequence of
RT its rfb gene cluster.";
RL J. Bacteriol. 176:4144-4156(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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 -!- INTERACTION:
CC P37745; P0A6F5: groEL; NbExp=3; IntAct=EBI-557071, EBI-543750;
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.
CC {ECO:0000305}.
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DR EMBL; U03041; AAC31630.1; -; Genomic_DNA.
DR EMBL; U09876; AAB88401.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75099.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15880.1; -; Genomic_DNA.
DR PIR; I69651; I69651.
DR RefSeq; NP_416542.1; NC_000913.3.
DR RefSeq; WP_001100981.1; NZ_LN832404.1.
DR AlphaFoldDB; P37745; -.
DR SMR; P37745; -.
DR BioGRID; 4261258; 244.
DR DIP; DIP-10681N; -.
DR IntAct; P37745; 3.
DR STRING; 511145.b2038; -.
DR jPOST; P37745; -.
DR PaxDb; P37745; -.
DR PRIDE; P37745; -.
DR EnsemblBacteria; AAC75099; AAC75099; b2038.
DR EnsemblBacteria; BAA15880; BAA15880; BAA15880.
DR GeneID; 947482; -.
DR KEGG; ecj:JW2023; -.
DR KEGG; eco:b2038; -.
DR PATRIC; fig|1411691.4.peg.213; -.
DR EchoBASE; EB1922; -.
DR eggNOG; COG1898; Bacteria.
DR HOGENOM; CLU_090940_1_1_6; -.
DR InParanoid; P37745; -.
DR OMA; RGVFLEW; -.
DR PhylomeDB; P37745; -.
DR BioCyc; EcoCyc:DTDPDEHYDRHAMEPIM-MON; -.
DR BioCyc; MetaCyc:DTDPDEHYDRHAMEPIM-MON; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR PRO; PR:P37745; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008830; F:dTDP-4-dehydrorhamnose 3,5-epimerase activity; ISS:UniProtKB.
DR GO; GO:0016854; F:racemase and epimerase activity; IBA:GO_Central.
DR GO; GO:0033692; P:cellular polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0019305; P:dTDP-rhamnose biosynthetic process; IBA:GO_Central.
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 GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Isomerase; Lipopolysaccharide biosynthesis;
KW Reference proteome.
FT CHAIN 1..185
FT /note="dTDP-4-dehydrorhamnose 3,5-epimerase"
FT /id="PRO_0000207978"
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 168
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 185 AA; 21270 MW; 60C50851A7046BA4 CRC64;
MNVIRTEIED VLILEPRVFG DDRGFFYESF NQSAFEHILG YPVSFVQDNH SRSSKNVLRG
LHFQRGEYAQ DKLVRCTHGA VFDVAVDIRP NSVSFGKWVG VLLSADNKQQ LWIPKGFAHG
FLVLSDIAEF QYKTTNYYHP ESDCGICWND ERIAIDWPQT SGLILSPKDE RLFTLDELIR
LKLIA
