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Protein

TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase

Gene

fdtA

Organism
Aneurinibacillus thermoaerophilus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei49Proton acceptor1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17003.
BRENDAi5.3.2.3. 344.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:fdtA
OrganismiAneurinibacillus thermoaerophilus
Taxonomic identifieri143495 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeAneurinibacillus groupAneurinibacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49H → N: Loss of catalytic activity. 1 Publication1
Mutagenesisi51H → N: Retains some catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004218231 – 139TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomeraseAdd BLAST139

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1139
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 13Combined sources4
Beta strandi16 – 22Combined sources7
Turni23 – 25Combined sources3
Beta strandi26 – 29Combined sources4
Beta strandi33 – 39Combined sources7
Beta strandi46 – 53Combined sources8
Beta strandi56 – 63Combined sources8
Beta strandi65 – 70Combined sources6
Beta strandi75 – 80Combined sources6
Beta strandi85 – 89Combined sources5
Beta strandi94 – 98Combined sources5
Beta strandi105 – 112Combined sources8
Helixi116 – 118Combined sources3
Helixi123 – 135Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PA7X-ray1.50A/B1-139[»]
2PAEX-ray2.50A/B1-139[»]
2PAKX-ray2.40A/B1-139[»]
2PAMX-ray2.50A/B1-139[»]
ProteinModelPortaliQ6T1W8.
SMRiQ6T1W8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6T1W8.

Family & Domainsi

Phylogenomic databases

KOiK20679.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR008894. WxcM_C.
[Graphical view]
PfamiPF05523. FdtA. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6T1W8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENKVINFKK IIDSRGSLVA IEENKNIPFS IKRVYYIFDT KGEEPRGFHA
60 70 80 90 100
HKKLEQVLVC LNGSCRVILD DGNIIQEITL DSPAVGLYVG PAVWHEMHDF
110 120 130
SSDCVMMVLA SDYYDETDYI RQYDNFKKYI AKINLEKEG
Length:139
Mass (Da):16,042
Last modified:July 5, 2004 - v1
Checksum:iEC32CB06F863F137
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY442352 Genomic DNA. Translation: AAS55720.1.

Genome annotation databases

KEGGiag:AAS55720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY442352 Genomic DNA. Translation: AAS55720.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PA7X-ray1.50A/B1-139[»]
2PAEX-ray2.50A/B1-139[»]
2PAKX-ray2.40A/B1-139[»]
2PAMX-ray2.50A/B1-139[»]
ProteinModelPortaliQ6T1W8.
SMRiQ6T1W8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAS55720.

Phylogenomic databases

KOiK20679.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17003.
BRENDAi5.3.2.3. 344.

Miscellaneous databases

EvolutionaryTraceiQ6T1W8.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR008894. WxcM_C.
[Graphical view]
PfamiPF05523. FdtA. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFDTA_ANETH
AccessioniPrimary (citable) accession number: Q6T1W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.