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B7LCQ5 (ULAD_ECO55) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:
3-keto-L-gulonate-6-phosphate decarboxylase UlaD

EC=4.1.1.85
Alternative name(s):
3-dehydro-L-gulonate-6-phosphate decarboxylase
KGPDC
L-ascorbate utilization protein D
Gene names
Name:ulaD
Ordered Locus Names:EC55989_4753
OrganismEscherichia coli (strain 55989 / EAEC) [Complete proteome] [HAMAP]
Taxonomic identifier585055 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization By similarity. HAMAP-Rule MF_01267

Catalytic activity

3-dehydro-L-gulonate 6-phosphate = L-xylulose 5-phosphate + CO2. HAMAP-Rule MF_01267

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01267

Pathway

Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 2/4. HAMAP-Rule MF_01267

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01267

Induction

Induced by L-ascorbate. Repressed by UlaR By similarity. HAMAP-Rule MF_01267

Sequence similarities

Belongs to the HPS/KGPDC family. KGPDC subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2162163-keto-L-gulonate-6-phosphate decarboxylase UlaD HAMAP-Rule MF_01267
PRO_1000165141

Sites

Metal binding331Magnesium By similarity
Metal binding621Magnesium By similarity
Binding site111Substrate By similarity
Binding site1921Substrate By similarity
Site641Transition state stabilizer By similarity
Site671Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
B7LCQ5 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: CDF287AC1D1BAD68

FASTA21623,649
        10         20         30         40         50         60 
MSLPMLQVAL DNQTMDSAYE TTRLIAEEVD IIEVGTILCV GEGVRAVRDL KALYPHKIVL 

        70         80         90        100        110        120 
ADAKIADAGK ILSRMCFEAN ADWVTVICCA DINTAKGALD VAKEFNGDVQ IELTGYWTWE 

       130        140        150        160        170        180 
QAQQWRDAGI QQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF 

       190        200        210 
KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU928145 Genomic DNA. Translation: CAV01690.1.
RefSeqYP_002405613.1. NC_011748.1.

3D structure databases

ProteinModelPortalB7LCQ5.
SMRB7LCQ5. Positions 2-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING585055.EC55989_4753.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAV01690; CAV01690; EC55989_4753.
GeneID7147915.
KEGGeck:EC55989_4753.
PATRIC38483098. VBIEscCol113220_4776.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0269.
HOGENOMHOG000226068.
KOK03078.
OMASHAYETT.
OrthoDBEOG66B435.

Enzyme and pathway databases

BioCycECOL585055:GJOM-4826-MONOMER.
UniPathwayUPA00263; UER00378.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01267. UlaD.
InterProIPR023942. 3-keto-L-gulonate6Pdecase_UlaD.
IPR013785. Aldolase_TIM.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
ProtoNetSearch...

Entry information

Entry nameULAD_ECO55
AccessionPrimary (citable) accession number: B7LCQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 42 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

PATHWAY comments

Index of metabolic and biosynthesis pathways