RMLD_BURTA
ID RMLD_BURTA Reviewed; 298 AA.
AC Q2SYI1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000250|UniProtKB:P26392};
DE EC=1.1.1.133 {ECO:0000305|PubMed:21640586};
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:0000303|PubMed:21640586};
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=rmlD {ECO:0000303|PubMed:21640586}; Synonyms=rfbD;
GN OrderedLocusNames=BTH_I1472;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=21640586; DOI=10.1016/j.bmcl.2011.05.030;
RA Yoo H.G., Kwon S.Y., Karki S., Kwon H.J.;
RT "A new route to dTDP-6-deoxy-l-talose and dTDP-L-rhamnose: dTDP-L-rhamnose
RT 4-epimerase in Burkholderia thailandensis.";
RL Bioorg. Med. Chem. Lett. 21:3914-3917(2011).
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 {ECO:0000269|PubMed:21640586}.
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:0000305|PubMed:21640586};
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:0000269|PubMed:21640586}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:21640586}.
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; CP000086; ABC37745.1; -; Genomic_DNA.
DR RefSeq; WP_009889586.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SYI1; -.
DR SMR; Q2SYI1; -.
DR PRIDE; Q2SYI1; -.
DR EnsemblBacteria; ABC37745; ABC37745; BTH_I1472.
DR KEGG; bte:BTH_I1472; -.
DR HOGENOM; CLU_045518_1_0_4; -.
DR OMA; FGEHGNN; -.
DR OrthoDB; 1076083at2; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0008831; F:dTDP-4-dehydrorhamnose reductase activity; IEA:UniProtKB-EC.
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: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 1: Evidence at protein level;
KW Carbohydrate metabolism; Lipopolysaccharide biosynthesis; Magnesium;
KW Metal-binding; NAD; NADP; Oxidoreductase.
FT CHAIN 1..298
FT /note="dTDP-4-dehydrorhamnose reductase"
FT /id="PRO_0000424104"
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 98
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 298 AA; 31631 MW; 19F9A0FAEC3AC923 CRC64;
MKILVTGANG QVGWELARSL AVLGQVVPLA RDEADLGRPE TLARIVEDAK PDVVVNAAAY
TAVDAAESDG AAAKVVNGEA VGVLAAATKR VGGLFVHYST DYVFDGTKSS PYIETDPTCP
VNAYGASKLL GELAVAETGG DWLTFRTTWV FAARGKNFLR TMLRLAKERE EMKIVADQFG
APTWARSIAD GTAHALATAM RERAAGAFTS GVYHMTSAGQ TSWHGFADAI VASWRAVPGA
APLAVSRIVP IPTSAYPVPA RRPANSVLSN EALKERFGIE LPDWRYAVGL CVRDLLSQ
