O27818 (RMLC_METTH) 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:	rmlC
Ordered Locus Names:	MTH_1790

Organism

Methanobacterium thermoautotrophicum (strain Delta H)

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

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. Ref.2
Catalytic activity	dTDP-4-dehydro-6-deoxy-D-glucose = dTDP-4-dehydro-6-deoxy-L-mannose. Ref.2
Pathway	Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.

Ontologies

Keywords
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	extracellular polysaccharide biosynthetic process Non-traceable author statement Ref.2. Source: UniProtKB lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	dTDP-4-dehydrorhamnose 3,5-epimerase activity Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

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_0000395351

Regions

Region

49 – 51

3

Substrate binding

Sites

Binding site

26

1

Substrate By similarity

Binding site

31

1

Substrate By similarity

Binding site

61

1

Substrate

Binding site

64

1

Substrate By similarity

Binding site

73

1

Substrate By similarity

Binding site

84

1

Substrate By similarity

Binding site

120

1

Substrate By similarity

Binding site

172

1

Substrate By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

185

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

15 – 19

5

Helix

35 – 40

6

Beta strand

49 – 56

8

Beta strand

63 – 69

7

Beta strand

74 – 79

6

Beta strand

82 – 87

6

Beta strand

102 – 104

3

Turn

106 – 108

3

Beta strand

111 – 113

3

Beta strand

122 – 124

3

Beta strand

126 – 137

12

Helix

141 – 143

3

Helix

160 – 162

3

Helix

170 – 173

4

Turn

178 – 180

3

Sequences

	Sequence		Length	Mass (Da)
	O27818 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: E321B0D881834139	FASTA	185	21,678
	10 20 30 40 50 60 MAEFRFIKTS LDGAIIIEPE VYTDERGYFM ETFNEAIFQE NGLEVRFVQD NESMSVRGVL 70 80 90 100 110 120 RGLHFQREKP QGKLVRVIRG EIFDVAVDLR KNSDTYGEWT GVRLSDENRR EFFIPEGFAH 130 140 150 160 170 180 GFLALSDECI VNYKCTELYH PEYDSGIPWD DPDIGIDWPL EMVDDLIISE KDRNWKPLRE NPVYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.
[2]	"Crystal structure of dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase from Methanobacterium thermoautotrophicum complexed with dTDP." Christendat D., Saridakis V., Dharamsi A., Bochkarev A., Pai E.F., Arrowsmith C.H., Edwards A.M. J. Biol. Chem. 275:24608-24612(2000) [PubMed: 10827167] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000666 Genomic DNA. Translation: AAB86256.1.

PIR

B69106.

RefSeq

NP_276896.1. NC_000916.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EP0	X-ray	1.50	A	1-185	[»]
1EPZ	X-ray	1.75	A	1-185	[»]

ProteinModelPortal

O27818.

SMR

O27818. Positions 3-185.

ModBase

Search...

Protein-protein interaction databases

STRING

O27818.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1470875.

GenomeReviews

Gene locus MTH_1790 in contig AE000666_GR.

KEGG

mth:MTH1790.

NMPDR

fig|187420.1.peg.1751.

Phylogenomic databases

eggNOG

arNOG08365.

HOGENOM

HBG730537.

OMA

VVEPRVF.

PhylomeDB

O27818.

ProtClustDB

CLSK2750672.

Enzyme and pathway databases

BioCyc

MTHE187420:MTH1790-MONOMER.

Family and domain databases

InterPro

IPR011051. Cupin_RmlC_type.
IPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]

Gene3D

G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.

KO

K01790.

PANTHER

PTHR21047. dTDP_sugar_isom. 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_METTH

Accession

Primary (citable) accession number: O27818

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program