Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5SFD1 (CHMJ_STRBI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
dTDP-4-dehydro-6-deoxyglucose 3-epimerase

EC=5.1.3.27
Alternative name(s):
dTDP-4-dehydro-6-deoxy-D-glucose 3-epimerase
dTDP-4-keto-6-deoxyglucose epimerase
dTDP-4-oxo-6-deoxy-D-glucose epimerase
Gene names
Name:chmJ
OrganismStreptomyces bikiniensis
Taxonomic identifier1896 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of dTDP-4-oxo-6-deoxyglucose to dTDP-4-oxo-6-deoxyallose, via a C-3 epimerization. This is a step in the biosynthesis of the mycinose moiety of the chalcomycin antibiotic. Ref.2

Catalytic activity

dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-allose. Ref.2

Subunit structure

Homodimer. Ref.2

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

kcat is 6.4 sec(-1).

KM=04 mM for dTDP-4-dehydro-6-deoxy-alpha-D-glucose

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196dTDP-4-dehydro-6-deoxyglucose 3-epimerase
PRO_0000425106

Sites

Active site601Proton acceptor Probable
Active site1301Proton donor Probable
Binding site211Substrate
Binding site261Substrate
Binding site451Substrate
Binding site571Substrate
Binding site701Substrate
Binding site1171Substrate
Binding site1361Substrate
Binding site1411Substrate

Experimental info

Mutagenesis601H → N: No effect on substrate affinity, but 2400-fold reduction in activity. Ref.2
Mutagenesis1301Y → F: Slight decrease in substrate affinity, and 1650-fold reduction in activity. Ref.2

Secondary structure

..................................... 196
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SFD1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 26C8CD880701F1CA

FASTA19621,683
        10         20         30         40         50         60 
MHPLSIEGAW SQEPVIHSDH RGRSHEWFRG ESFRQAFGHD FPVAQVNVAV SHRGALRGIH 

        70         80         90        100        110        120 
YTEIPPGQAK YSVCVRGAGL DVVVDVRIGS PTFGRWEIVP MDAERNTAVY LTAGLGRAFL 

       130        140        150        160        170        180 
SLTDDATLVY LCSSGYAPAR EHSVNPLDPD LGIAWPDDIE PLLSDRDENA PTLATAERLG 

       190 
LLPTYQAWQE QQQAQR 

« Hide

References

[1]"Chalcomycin biosynthesis gene cluster from Streptomyces bikiniensis: novel features of an unusual ketolide produced through expression of the chm polyketide synthase in Streptomyces fradiae."
Ward S.L., Hu Z., Schirmer A., Reid R., Revill W.P., Reeves C.D., Petrakovsky O.V., Dong S.D., Katz L.
Antimicrob. Agents Chemother. 48:4703-4712(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NRRL 2737.
[2]"Structural and functional studies on a 3'-epimerase involved in the biosynthesis of dTDP-6-deoxy-D-allose."
Kubiak R.L., Phillips R.K., Zmudka M.W., Ahn M.R., Maka E.M., Pyeatt G.L., Roggensack S.J., Holden H.M.
Biochemistry 51:9375-9383(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF APOENZYME; COMPLEX WITH DTDP-QUINOVOSE AND MUTANT ASN-60/PHE-130 IN COMPLEX WITH DTDP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITES, MUTAGENESIS OF HIS-60 AND TYR-130.
Strain: NRRL 2737.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY509120 Genomic DNA. Translation: AAS79451.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HMZX-ray2.00A/B/C/D1-196[»]
4HN0X-ray2.20A/B/C/D1-196[»]
4HN1X-ray1.60A/B/C/D1-196[»]
ProteinModelPortalQ5SFD1.
SMRQ5SFD1. Positions 2-189.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. SSF51182. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCHMJ_STRBI
AccessionPrimary (citable) accession number: Q5SFD1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references