P37760 (RMLD_ECOLI) 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
Ordered Locus Names:	b2040, JW2025

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 By similarity.
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
Technical term	Complete proteome Reference proteome
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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 299	299	dTDP-4-dehydrorhamnose reductase		PRO_0000207984
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	128 – 132	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	153	1	Substrate; via amide nitrogen By similarity
	Binding site	154	1	NAD; via amide nitrogen By similarity
	Binding site	223	1	Substrate By similarity
	Binding site	260	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37760 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 1D7C992FA5017AD1	FASTA	299	32,694
	10 20 30 40 50 60 MNILLFGKTG QVGWELQRAL APLGNLIAFD VHSTDYCGDF SNPEGVAETV RSIRPDIIVN 70 80 90 100 110 120 AAAHTAVDKA ESEPEFAQLI NATSVEAIAK AANEVGAWVI HYSTDYVFPG NGDMPWLETD 130 140 150 160 170 180 ATAPLNVYGE TKLAGEKALQ EYCAKHLIFR TSWVYAGKGN NFAKTMLRLA KEREELAVIN 190 200 210 220 230 240 DQFGAPTGAE LLADCTAHAI RVALNKPDVA GLYHLVASGT TTWYDYAALV FEEARKAGIP 250 260 270 280 290 LALNKLNAVP TTAYPTPARR PHNSRLNTEK FQQNFALVLP DWQVGVKRML NELFTTTAI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the O antigen of Escherichia coli K-12 and the sequence of its rfb gene cluster." Stevenson G., Neal B., Liu D., Hobbs M., Packer N.H., Batley M., Redmond J.W., Lindquist L., Reeves P.R. J. Bacteriol. 176:4144-4156(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / WG1.
[2]	Stevenson G. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 227.
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09876 Genomic DNA. Translation: AAB88399.1. U00096 Genomic DNA. Translation: AAC75101.1. AP009048 Genomic DNA. Translation: BAA15882.1.
PIR	G64969.
RefSeq	NP_416544.1. NC_000913.2. YP_490282.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P37760.
SMR	P37760. Positions 1-297.
ModBase	Search...
Protein-protein interaction databases
IntAct	P37760. 5 interactions.
STRING	511145.b2040.
Proteomic databases
PRIDE	P37760.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75101; AAC75101; b2040. BAA15882; BAA15882; BAA15882.
GeneID	12932555. 947117.
KEGG	ecj:Y75_p2003. eco:b2040.
PATRIC	32119413. VBIEscCol129921_2117.
Organism-specific databases
EchoBASE	EB2310.
EcoGene	EG12411. rfbD.
Phylogenomic databases
HOGENOM	HOG000227712.
KO	K00067.
OMA	KNFIKTM.
ProtClustDB	PRK09987.
Enzyme and pathway databases
BioCyc	EcoCyc:DTDPDEHYRHAMREDUCT-MONOMER. ECOL316407:JW2025-MONOMER. MetaCyc:DTDPDEHYRHAMREDUCT-MONOMER.
UniPathway	UPA00124. UPA00281.
Gene expression databases
Genevestigator	P37760.
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_ECOLI

Accession

Primary (citable) accession number: P37760
Secondary accession number(s): P76377

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program