RMLD_ECOLI
ID RMLD_ECOLI Reviewed; 299 AA.
AC P37760; P76377;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000250|UniProtKB:P26392};
DE EC=1.1.1.133 {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-4-keto-L-rhamnose reductase {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-6-deoxy-L-lyxo-4-hexulose reductase {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-6-deoxy-L-mannose dehydrogenase {ECO:0000250|UniProtKB:P26392};
DE AltName: Full=dTDP-L-rhamnose synthase {ECO:0000250|UniProtKB:P26392};
GN Name=rfbD {ECO:0000303|PubMed:7517391}; Synonyms=rmlD;
GN OrderedLocusNames=b2040, JW2025;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
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 [2]
RP SEQUENCE REVISION TO 227.
RA Stevenson G.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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: Involved in the biosynthesis of the dTDP-L-rhamnose which is
CC an important component of lipopolysaccharide (LPS) (Probable).
CC Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield
CC dTDP-L-rhamnose (By similarity). RmlD uses NADH and NADPH nearly
CC equally well (By similarity). {ECO:0000250|UniProtKB:P26392,
CC ECO:0000305|PubMed:7517391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-
CC rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:21796, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57510, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:62830; EC=1.1.1.133;
CC Evidence={ECO:0000250|UniProtKB:P26392};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P26392};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P26392};
CC -!- PATHWAY: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
CC {ECO:0000305|PubMed:7517391}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000305|PubMed:7517391}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26392}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC {ECO:0000305}.
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DR EMBL; U09876; AAB88399.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75101.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15882.1; -; Genomic_DNA.
DR PIR; G64969; G64969.
DR RefSeq; NP_416544.1; NC_000913.3.
DR RefSeq; WP_001023610.1; NZ_LN832404.1.
DR AlphaFoldDB; P37760; -.
DR SMR; P37760; -.
DR BioGRID; 4261549; 180.
DR IntAct; P37760; 5.
DR STRING; 511145.b2040; -.
DR jPOST; P37760; -.
DR PaxDb; P37760; -.
DR PRIDE; P37760; -.
DR EnsemblBacteria; AAC75101; AAC75101; b2040.
DR EnsemblBacteria; BAA15882; BAA15882; BAA15882.
DR GeneID; 947117; -.
DR KEGG; ecj:JW2025; -.
DR KEGG; eco:b2040; -.
DR PATRIC; fig|511145.12.peg.2117; -.
DR EchoBASE; EB2310; -.
DR eggNOG; COG1091; Bacteria.
DR HOGENOM; CLU_045518_1_0_6; -.
DR InParanoid; P37760; -.
DR OMA; AGETTWH; -.
DR PhylomeDB; P37760; -.
DR BioCyc; EcoCyc:DTDPDEHYRHAMREDUCT-MON; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR PRO; PR:P37760; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; PTHR10491; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01214; rmlD; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Lipopolysaccharide biosynthesis; Magnesium;
KW Metal-binding; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..299
FT /note="dTDP-4-dehydrorhamnose reductase"
FT /id="PRO_0000207984"
FT ACT_SITE 128
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 10..12
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 11..12
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 30
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 39..40
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 39..40
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 63..65
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 63..65
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 102
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 104..105
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 128
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 128
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 132
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 132
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 153
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT SITE 104
FT /note="Could provide a fine-tuning to achieve optimal pKa
FT matching between active site and substrate"
FT /evidence="ECO:0000250|UniProtKB:P26392"
SQ SEQUENCE 299 AA; 32694 MW; 1D7C992FA5017AD1 CRC64;
MNILLFGKTG QVGWELQRAL APLGNLIAFD VHSTDYCGDF SNPEGVAETV RSIRPDIIVN
AAAHTAVDKA ESEPEFAQLI NATSVEAIAK AANEVGAWVI HYSTDYVFPG NGDMPWLETD
ATAPLNVYGE TKLAGEKALQ EYCAKHLIFR TSWVYAGKGN NFAKTMLRLA KEREELAVIN
DQFGAPTGAE LLADCTAHAI RVALNKPDVA GLYHLVASGT TTWYDYAALV FEEARKAGIP
LALNKLNAVP TTAYPTPARR PHNSRLNTEK FQQNFALVLP DWQVGVKRML NELFTTTAI
