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Reviewed, UniProtKB/Swiss-Prot Q0T9J7 (ULAD_ECOL5)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: ECP_4441
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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.

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

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

Subunit structure

Homodimer By similarity.

Induction

Induced by L-ascorbate. Repressed by ulaR By similarity.

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 MF_01267
PRO_1000067320

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
Q0T9J7-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: EC8490DA1D02D824

FASTA21623,578
        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 GQVVYHRSRD AQAAGVAWGE ADITAIKRLS DMGFKVTVTG GLALEDLPLF 

       190        200        210 
KGIPIHVFIA GRSIRDAASP VEAARQFKRS IAELWG 

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000247 Genomic DNA. Translation: ABG72382.1.
RefSeqYP_672283.1.

3D structure databases

SMRQ0T9J7. Positions 2-216.
ModBaseSearch...

Genome annotation databases

GeneID4190033.
GenomeReviewsGene locus ECP_4441 in contig CP000247_GR.
KEGGecp:ECP_4441.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0T9J7.
OMAQ0T9J7. PIYIFIA.

Enzyme and pathway databases

BioCycECOL362663:ECP_4441-MON.

Family and domain databases

HAMAPMF_01267.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR001754. OMPdecase_core.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF00215. OMPdecase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameULAD_ECOL5
AccessionPrimary (citable) accession number: Q0T9J7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents