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Q6T1W8 (FDTA_ANETH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase

EC=5.3.2.3
Alternative name(s):
dTDP-6-deoxy-3,4-keto-hexulose isomerase
Gene names
Name:fdtA
OrganismAneurinibacillus thermoaerophilus
Taxonomic identifier143495 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeAneurinibacillus groupAneurinibacillus

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the isomerization of dTDP-6-deoxy-D-xylohex-4-ulose into dTDP-6-deoxy-D-xylohex-3-ulose in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose, a glycan chain of the S-layer. Ref.1 Ref.2

Catalytic activity

dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose = dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose. Ref.1 Ref.2

Subunit structure

Homodimer. Ref.2

Ontologies

Keywords
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Molecular_functionisomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 139139TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase
PRO_0000421823

Sites

Active site491Proton acceptor Probable

Experimental info

Mutagenesis491H → N: Loss of catalytic activity. Ref.2
Mutagenesis511H → N: Retains some catalytic activity. Ref.2

Secondary structure

............................. 139
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q6T1W8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EC32CB06F863F137

FASTA13916,042
        10         20         30         40         50         60 
MENKVINFKK IIDSRGSLVA IEENKNIPFS IKRVYYIFDT KGEEPRGFHA HKKLEQVLVC 

        70         80         90        100        110        120 
LNGSCRVILD DGNIIQEITL DSPAVGLYVG PAVWHEMHDF SSDCVMMVLA SDYYDETDYI 

       130 
RQYDNFKKYI AKINLEKEG 

« Hide

References

[1]"Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose in Aneurinibacillus thermoaerophilus L420-91T."
Pfoestl A., Hofinger A., Kosma P., Messner P.
J. Biol. Chem. 278:26410-26417(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
Strain: L420-91T.
[2]"The x-ray structure of dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase."
Davis M.L., Thoden J.B., Holden H.M.
J. Biol. Chem. 282:19227-19236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS), SUBUNIT, ACTIVE SITE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-49 AND HIS-51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY442352 Genomic DNA. Translation: AAS55720.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PA7X-ray1.50A/B1-139[»]
2PAEX-ray2.50A/B1-139[»]
2PAKX-ray2.40A/B1-139[»]
2PAMX-ray2.50A/B1-139[»]
ProteinModelPortalQ6T1W8.
SMRQ6T1W8. Positions 2-136.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17003.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR008894. WxcM_C.
[Graphical view]
PfamPF05523. FdtA. 1 hit.
[Graphical view]
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ6T1W8.

Entry information

Entry nameFDTA_ANETH
AccessionPrimary (citable) accession number: Q6T1W8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references