P37745 (RMLC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
dTDP-4-dehydrorhamnose 3,5-epimerase
EC=5.1.3.13

Alternative name(s):
Thymidine diphospho-4-keto-rhamnose 3,5-epimerase
dTDP-4-keto-6-deoxyglucose 3,5-epimerase
dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase
dTDP-L-rhamnose synthase

Gene names

Name:	rfbC
Synonyms:	rmlC
Ordered Locus Names:	b2038, JW2023

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	185 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose By similarity.
Catalytic activity	dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-beta-L-mannose.
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 3,5-epimerase family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Molecular function	Isomerase
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 response to DNA damage stimulus Inferred from mutant phenotype PubMed 20128927. Source: EcoCyc response to antibiotic Inferred from mutant phenotype PubMed 20128927. Source: EcoCyc
Molecular_function	dTDP-4-dehydrorhamnose 3,5-epimerase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	2	EBI-557071,EBI-543750

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 185	185	dTDP-4-dehydrorhamnose 3,5-epimerase		PRO_0000207978
Regions
	Region	168 – 169	2	Substrate binding By similarity
Sites
	Binding site	23	1	Substrate By similarity
	Binding site	28	1	Substrate By similarity
	Binding site	47	1	Substrate By similarity
	Binding site	49	1	Substrate By similarity
	Binding site	59	1	Substrate By similarity
	Binding site	62	1	Substrate By similarity
	Binding site	72	1	Substrate By similarity
	Binding site	83	1	Substrate By similarity
	Binding site	119	1	Substrate By similarity
	Site	62	1	Important in abstrating the protons in C3' and C5' By similarity
	Site	132	1	May have a key role in proton donation to C5' By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37745 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 60C50851A7046BA4	FASTA	185	21,270
	10 20 30 40 50 60 MNVIRTEIED VLILEPRVFG DDRGFFYESF NQSAFEHILG YPVSFVQDNH SRSSKNVLRG 70 80 90 100 110 120 LHFQRGEYAQ DKLVRCTHGA VFDVAVDIRP NSVSFGKWVG VLLSADNKQQ LWIPKGFAHG 130 140 150 160 170 180 FLVLSDIAEF QYKTTNYYHP ESDCGICWND ERIAIDWPQT SGLILSPKDE RLFTLDELIR LKLIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a." Yao Z., Valvano M.A. J. Bacteriol. 176:4133-4143(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U03041 Genomic DNA. Translation: AAC31630.1. U09876 Genomic DNA. Translation: AAB88401.1. U00096 Genomic DNA. Translation: AAC75099.1. AP009048 Genomic DNA. Translation: BAA15880.1.
PIR	I69651.
RefSeq	NP_416542.1. NC_000913.2. YP_490280.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P37745.
SMR	P37745. Positions 1-179.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10681N.
IntAct	P37745. 3 interactions.
MINT	MINT-1257696.
STRING	511145.b2038.
Proteomic databases
PaxDb	P37745.
PRIDE	P37745.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75099; AAC75099; b2038. BAA15880; BAA15880; BAA15880.
GeneID	12932264. 947482.
KEGG	ecj:Y75_p2001. eco:b2038.
PATRIC	32119409. VBIEscCol129921_2114.
Organism-specific databases
EchoBASE	EB1922.
EcoGene	EG11979. rfbC.
Phylogenomic databases
eggNOG	COG1898.
HOGENOM	HOG000227724.
KO	K01790.
OMA	VIIEPRV.
ProtClustDB	CLSK2301700.
Enzyme and pathway databases
BioCyc	EcoCyc:DTDPDEHYDRHAMEPIM-MONOMER. ECOL316407:JW2023-MONOMER. MetaCyc:DTDPDEHYDRHAMEPIM-MONOMER.
UniPathway	UPA00124. UPA00281.
Gene expression databases
Genevestigator	P37745.
Family and domain databases
Gene3D	2.60.120.10. 1 hit.
InterPro	IPR000888. dTDP_sugar_isom. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR21047. PTHR21047. 1 hit.
Pfam	PF00908. dTDP_sugar_isom. 1 hit. [Graphical view]
ProDom	PD001462. dTDP_sugar_isom. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR01221. rmlC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RMLC_ECOLI

Accession

Primary (citable) accession number: P37745

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program