RMLD_AGGAC
ID RMLD_AGGAC Reviewed; 294 AA.
AC O66251;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=dTDP-4-dehydrorhamnose reductase {ECO:0000250|UniProtKB:P26392};
DE EC=1.1.1.133 {ECO:0000269|PubMed:10702238};
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:10702238};
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:9805002};
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33384 / DSM 8324 / CCUG 13227 / NCTC 9710 / Serotype c;
RX PubMed=9805002; DOI=10.1016/s0167-4781(98)00174-2;
RA Nakano Y., Yoshida Y., Yamashita Y., Koga T.;
RT "A gene cluster for 6-deoxy-L-talan synthesis in Actinobacillus
RT actinomycetemcomitans.";
RL Biochim. Biophys. Acta 1442:409-414(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 33384 / DSM 8324 / CCUG 13227 / NCTC 9710 / Serotype c;
RX PubMed=10702238; DOI=10.1074/jbc.275.10.6806;
RA Nakano Y., Suzuki N., Yoshida Y., Nezu T., Yamashita Y., Koga T.;
RT "Thymidine diphosphate-6-deoxy-L-lyxo-4-hexulose reductase synthesizing
RT dTDP-6-deoxy-L-talose from Actinobacillus actinomycetemcomitans.";
RL J. Biol. Chem. 275:6806-6812(2000).
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:10702238}.
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:0000269|PubMed:10702238};
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:10702238}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:10702238}.
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; AB010415; BAA28133.1; -; Genomic_DNA.
DR PIR; T00104; T00104.
DR RefSeq; WP_005574038.1; NZ_VSEV01000001.1.
DR AlphaFoldDB; O66251; -.
DR SMR; O66251; -.
DR BioCyc; MetaCyc:MON-18135; -.
DR UniPathway; UPA00124; -.
DR UniPathway; UPA00281; -.
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..294
FT /note="dTDP-4-dehydrorhamnose reductase"
FT /id="PRO_0000424093"
FT ACT_SITE 127
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 11..13
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 12..13
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 38..39
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 38..39
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 62..64
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 62..64
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 103..104
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 127
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 127
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 131
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 131
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT BINDING 152
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:P26392"
FT SITE 103
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 294 AA; 32356 MW; 669171C84964B094 CRC64;
MARLLITGAG GQLGRSLAKL LVDNGRYEVL ALDFSELDIT NKDMVFSIID SFKPNVIINA
AAYTSVDQAE LEVSSAYSVN VRGVQYLAEA AIRHNSAILH VSTDYVFDGY KSGKYKETDI
IHPLCVYGKS KAEGERLLLT LSPKSIILRT SWTFGEYGNN FVKTMLRLAK NRDILGVVAD
QIGGPTYSGD IASVLIQIAE KIIVGETVKY GIYHFTGEPC VSWYDFAIAI FDEAVAQKVL
ENVPLVNAIT TADYPTLAKR PANSCLDLTK IQQAFGIQPS DWQRALKNIR AYAE
