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Reviewed, UniProtKB/Swiss-Prot Q0T9J6 (ULAE_ECOL5)

Last modified June 16, 2009. Version 24. 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:
    L-ribulose-5-phosphate 3-epimerase ulaE
    EC=5.1.3.22
Alternative name(s):
    L-xylulose-5-phosphate 3-epimerase
    L-ascorbate utilization protein E
Gene names
Name: ulaE
Ordered Locus Names: ECP_4442
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization By similarity.

Catalytic activity

L-ribulose 5-phosphate = L-xylulose 5-phosphate. HAMAP MF_01951

Pathway

Cofactor degradation; L-ascorbic acid degradation; D-xylulose 5-phosphate from L-ascorbic acid: step 3/4. HAMAP MF_01951

Induction

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

Sequence similarities

Belongs to the HUMPI family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284L-ribulose-5-phosphate 3-epimerase ulaE HAMAP MF_01951
PRO_1000070633

Sequences

Sequence LengthMass (Da)Tools
Q0T9J6-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 31CA9644DC4A8529

FASTA28432,035
        10         20         30         40         50         60 
MLSKQIPLGI YEKALPAGEC WLERLQLAKT LGFDFVEMSV DETDDRLSRL DWSREQRLAL 

        70         80         90        100        110        120 
VNAIVETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR KAIQFAQDVG IRVIQLAGYD 

       130        140        150        160        170        180 
VYYQEANNET RRRFRDGLKE SVEMASRAQV TLAMEIMDYP LMNSISKALG YAHYLNNPWF 

       190        200        210        220        230        240 
QLYPDIGNLS AWDNDVQMEL QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK 

       250        260        270        280 
QSGYCGPYLI EMWSETAEDP AAEVAKARDW VKARMAKAGM VEAA 

« 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: ABG72383.1.
RefSeqYP_672284.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4190034.
GenomeReviewsGene locus ECP_4442 in contig CP000247_GR.
KEGGecp:ECP_4442.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0T9J6.
OMAQ0T9J6. VVKARDW.

Enzyme and pathway databases

BioCycECOL362663:ECP_4442-MON.

Family and domain databases

HAMAPMF_01951.
[Tree]
InterProIPR004560. Hxl6Piso_put.
IPR013022. Xyl_isomerase-like_TIM-brl.
IPR012307. Xyl_isomerase-typ_TIM-brl.
[Graphical view]
Gene3DG3DSA:3.20.20.150. Xyl_isomerase-like_TIM-brl. 1 hit.
PfamPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00542. hxl6Piso_put. 1 hit.
ProtoNetSearch...

Entry information

Entry nameULAE_ECOL5
AccessionPrimary (citable) accession number: Q0T9J6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: June 16, 2009
This is version 24 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