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Reviewed, UniProtKB/Swiss-Prot Q1R363 (ULAE_ECOUT)

Last modified June 16, 2009. Version 22. 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: UTI89_C4797
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [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_1000070634

Sequences

Sequence LengthMass (Da)Tools
Q1R363-1 [UniParc].

Last modified May 16, 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]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000243 Genomic DNA. Translation: ABE10201.1.
RefSeqYP_543732.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3989836.
GenomeReviewsGene locus UTI89_C4797 in contig CP000243_GR.
KEGGeci:UTI89_C4797.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1R363.
OMAQ1R363. VVKARDW.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C4797-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_ECOUT
AccessionPrimary (citable) accession number: Q1R363
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 22 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