ID   RMLD_SINFN              Reviewed;         296 AA.
AC   P55463;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 129.
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   OrderedLocusNames=NGR_a03570; ORFNames=y4gG;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Involved in the biosynthesis of the dTDP-L-rhamnose which is
CC       an important component of lipopolysaccharide (LPS). Catalyzes the
CC       reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
CC       RmlD uses NADH and NADPH nearly equally well.
CC       {ECO:0000250|UniProtKB:P26392}.
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:0000250|UniProtKB:P37760}.
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; U00090; AAB91681.1; -; Genomic_DNA.
DR   RefSeq; NP_443869.1; NC_000914.2.
DR   RefSeq; WP_010875371.1; NC_000914.2.
DR   AlphaFoldDB; P55463; -.
DR   SMR; P55463; -.
DR   STRING; 394.NGR_a03570; -.
DR   EnsemblBacteria; AAB91681; AAB91681; NGR_a03570.
DR   KEGG; rhi:NGR_a03570; -.
DR   PATRIC; fig|394.7.peg.365; -.
DR   eggNOG; COG1091; Bacteria.
DR   HOGENOM; CLU_045518_1_2_5; -.
DR   OMA; AGETTWH; -.
DR   OrthoDB; 1076083at2; -.
DR   UniPathway; UPA00124; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
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; Magnesium; Metal-binding; NAD; NADP;
KW   Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..296
FT                   /note="dTDP-4-dehydrorhamnose reductase"
FT                   /id="PRO_0000207988"
FT   ACT_SITE        124
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         35..36
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         35..36
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         59..61
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         59..61
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         100..101
FT                   /ligand="dTDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:57510"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         124
FT                   /ligand="NADH"
FT                   /ligand_id="ChEBI:CHEBI:57945"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   BINDING         124
FT                   /ligand="NADPH"
FT                   /ligand_id="ChEBI:CHEBI:57783"
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         149
FT                   /ligand="dTDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:57510"
FT                   /evidence="ECO:0000250|UniProtKB:P26392"
FT   SITE            100
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   296 AA;  32236 MW;  36B97283479F2164 CRC64;
     MRLAVTGKNG QIALALKAQA RPDVEILTLG RPNFDLACRS TVASSIRDAA PDIIVSLAAY
     TAVDKAESEP YEAFAVNRDG VQALAEAAAG LGVPVIHLST DYVFDGAKPV PYCEEDRTGP
     ISVYGRSKLE GEFAVASANP NHTILRTSWV YSRYGQNFVK KMLRLADTND ELNVVADQLG
     CPTSADDISV AVMTIARRML SSSSADLRGI FHLSGSGEAS WAAFAKYVFS VYDEITGRQI
     KVHDISAAEY PTPARRPANS RLHCDKLERT FGIRLPNWEE STRRLVWALL LEGKDA