Q46769 (RMLD_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
dTDP-4-dehydrorhamnose reductase
EC=1.1.1.133

Alternative name(s):
dTDP-4-keto-L-rhamnose reductase
dTDP-6-deoxy-L-lyxo-4-hexulose reductase
dTDP-6-deoxy-L-mannose dehydrogenase
dTDP-L-rhamnose synthase

Gene names

Name:	rfbD
Synonyms:	rmlD

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well. Ref.1
Catalytic activity	dTDP-6-deoxy-beta-L-mannose + NADP+ = dTDP-4-dehydro-6-deoxy-beta-L-mannose + NADPH.
Cofactor	Binds 1 magnesium ion per monomer By similarity.
Pathway	Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the dTDP-4-dehydrorhamnose reductase family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	O antigen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dTDP-rhamnose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway extracellular polysaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB lipopolysaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	dTDP-4-dehydrorhamnose reductase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	dTDP-4-dehydrorhamnose reductase		PRO_0000207985
Regions
	Nucleotide binding	7 – 11	5	NAD By similarity
	Nucleotide binding	11 – 12	2	NADP By similarity
	Nucleotide binding	30 – 31	2	NAD By similarity
	Nucleotide binding	39 – 40	2	NAD/NADP By similarity
	Nucleotide binding	62 – 65	4	NAD By similarity
	Nucleotide binding	63 – 65	3	NADP By similarity
	Nucleotide binding	129 – 133	5	NAD/NADP By similarity
	Region	104 – 105	2	Substrate binding By similarity
Sites
	Binding site	12	1	NAD; via amide nitrogen By similarity
	Binding site	102	1	NADP; via carbonyl oxygen By similarity
	Binding site	155	1	Substrate; via amide nitrogen By similarity
	Binding site	156	1	NAD; via amide nitrogen By similarity
	Binding site	225	1	Substrate By similarity
	Binding site	262	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q46769 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A1C4271C20AB4A13	FASTA	301	32,866
	10 20 30 40 50 60 MNILLFGKTG QVGWELQRAL APLGNLIALD VHSTDYCGDF SNPEGVAETV KKIRPDVIVN 70 80 90 100 110 120 AAAHTDVDKA ESEPEFAQLL NATSVEAIAK AANEVGAWVI HYSTDYVFPG TGEIPWQGGT 130 140 150 160 170 180 DATAPLNVYG ETKLSSEKKA LQKHCGKHII FRTSWVYAGK GNNFAKTMLR LAKEREELAV 190 200 210 220 230 240 INDQFGRPTG AELLADCTAH AIRVAVDKPE VAGLYHLVAG GTTTWHDYAA LVFEEARKAG 250 260 270 280 290 300 INLALNKLNA VPTTAYPTPA RRPHNSRLNT EKFQQNFALV LPDWQVGVKR MLNELFTTTA I

References

[1]

"Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene." Marolda C.L., Valvano M.A. J. Bacteriol. 177:5539-5546(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS. Strain: O7:K1 / VW187.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF125322 Genomic DNA. Translation: AAC63613.1.
PIR	S78543.
3D structure databases
ProteinModelPortal	Q46769.
SMR	Q46769. Positions 1-299.
ModBase	Search...
Proteomic databases
PaxDb	Q46769.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG1091.
Enzyme and pathway databases
UniPathway	UPA00124. UPA00281.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR005913. dTDP_dehydrorham_reduct. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF04321. RmlD_sub_bind. 1 hit. [Graphical view]
TIGRFAMs	TIGR01214. rmlD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RMLD_ECOLX

Accession

Primary (citable) accession number: Q46769

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program