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P26394 (RMLC_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:STM2094
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Protein existenceEvidence 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.3

Catalytic activity

dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-beta-L-mannose. Ref.3

Pathway

Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.

Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.

Subunit structure

Homodimer. Ref.4

Sequence similarities

Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 183183dTDP-4-dehydrorhamnose 3,5-epimerase
PRO_0000207979

Regions

Region169 – 1702Substrate binding

Sites

Binding site241Substrate
Binding site291Substrate
Binding site481Substrate
Binding site501Substrate By similarity
Binding site601Substrate
Binding site631Substrate By similarity
Binding site731Substrate By similarity
Binding site841Substrate By similarity
Binding site1201Substrate By similarity
Site631Important in abstrating the protons in C3' and C5'
Site1331May have a key role in proton donation to C5'

Experimental info

Mutagenesis631H → A: Loss of epimerase activity. Ref.3
Mutagenesis731K → A: Reduces the epimerase activity by over 100-fold. Ref.3
Mutagenesis1331Y → F: Reduces the epimerase activity by over 1000-fold. Ref.3

Secondary structure

1 ...................................... 183
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26394 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 0176B52C38038C77

FASTA18320,663
        10         20         30         40         50         60 
MMIVIKTAIP DVLILEPKVF GDERGFFFES YNQQTFEELI GRKVTFVQDN HSKSKKNVLR 

        70         80         90        100        110        120 
GLHFQRGENA QGKLVRCAVG EVFDVAVDIR KESPTFGQWV GVNLSAENKR QLWIPEGFAH 

       130        140        150        160        170        180 
GFVTLSEYAE FLYKATNYYS PSSEGSILWN DEAIGIEWPF SQLPELSAKD AAAPLLDQAL 


LTE

« Hide

References

« Hide 'large scale' references
[1]"Structure and sequence of the rfb (O antigen) gene cluster of Salmonella serovar typhimurium (strain LT2)."
Jiang X.-M., Neal B., Santiago F., Lee S.J., Romana L.K., Reeves P.R.
Mol. Microbiol. 5:695-713(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"RmlC, a C3' and C5' carbohydrate epimerase, appears to operate via an intermediate with an unusual twist boat conformation."
Dong C., Major L.L., Srikannathasan V., Errey J.C., Giraud M.F., Lam J.S., Graninger M., Messner P., McNeil M.R., Field R.A., Whitfield C., Naismith J.H.
J. Mol. Biol. 365:146-159(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-63; LYS-73 AND TYR-133, FUNCTION IN DTDP-RHAMNOSE BIOSYNTHESIS, CATALYTIC ACTIVITY, REACTION MECHANISM.
[4]"RmlC, the third enzyme of dTDP-L-rhamnose pathway, is a new class of epimerase."
Giraud M.-F., Leonard G.A., Field R.A., Berlind C., Naismith J.H.
Nat. Struct. Biol. 7:398-402(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X56793 Genomic DNA. Translation: CAA40118.1.
AE006468 Genomic DNA. Translation: AAL20998.1.
PIRS15302.
RefSeqNP_461039.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DZRX-ray2.17A/B1-183[»]
1DZTX-ray2.20A/B1-183[»]
ProteinModelPortalP26394.
SMRP26394. Positions 1-183.
ModBaseSearch...

Protein-protein interaction databases

STRING99287.STM2094.

Proteomic databases

PaxDbP26394.
PRIDEP26394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20998; AAL20998; STM2094.
GeneID1253615.
KEGGstm:STM2094.
PATRIC32382771. VBISalEnt20916_2216.

Phylogenomic databases

eggNOGCOG1898.
HOGENOMHOG000227724.
KOK01790.
OMAVIIEPRV.
ProtClustDBCLSK894272.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2106-MONOMER.
SABIO-RKP26394.
UniPathwayUPA00124.
UPA00281.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR000888. dTDP_sugar_isom.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERPTHR21047. PTHR21047. 1 hit.
PfamPF00908. dTDP_sugar_isom. 1 hit.
[Graphical view]
ProDomPD001462. dTDP_sugar_isom. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMsTIGR01221. rmlC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP26394.

Entry information

Entry nameRMLC_SALTY
AccessionPrimary (citable) accession number: P26394
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 29, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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