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Protein

L-ribulose-5-phosphate 3-epimerase UlaE

Gene

ulaE

Organism
Shigella flexneri serotype 5b (strain 8401)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

Catalytic activityi

L-ribulose 5-phosphate = L-xylulose 5-phosphate.UniRule annotation

Pathwayi: L-ascorbate degradation

This protein is involved in step 3 of the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Probable L-ascorbate-6-phosphate lactonase UlaG (yjfR)
  2. 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (ulaD)
  3. L-ribulose-5-phosphate 3-epimerase UlaE (ulaE)
  4. L-ribulose-5-phosphate 4-epimerase UlaF (ulaF)
This subpathway is part of the pathway L-ascorbate degradation, which is itself part of Cofactor degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-xylulose 5-phosphate from L-ascorbate, the pathway L-ascorbate degradation and in Cofactor degradation.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase

Enzyme and pathway databases

BioCyciSFLE373384:G1G64-5074-MONOMER
UniPathwayiUPA00263; UER00379

Names & Taxonomyi

Protein namesi
Recommended name:
L-ribulose-5-phosphate 3-epimerase UlaEUniRule annotation (EC:5.1.3.22UniRule annotation)
Alternative name(s):
L-ascorbate utilization protein EUniRule annotation
L-xylulose-5-phosphate 3-epimeraseUniRule annotation
Gene namesi
Name:ulaEUniRule annotation
Ordered Locus Names:SFV_4353
OrganismiShigella flexneri serotype 5b (strain 8401)
Taxonomic identifieri373384 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000000659 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000706351 – 284L-ribulose-5-phosphate 3-epimerase UlaEAdd BLAST284

Expressioni

Inductioni

Induced by L-ascorbate. Repressed by UlaR.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ0SX88
SMRiQ0SX88
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-ribulose-5-phosphate 3-epimerase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000126090
KOiK03079
OMAiQAGMGHI

Family and domain databases

HAMAPiMF_01951 UlaE, 1 hit
InterProiView protein in InterPro
IPR004560 L-Ru-5P_3-Epase
IPR023492 L-Ru-5P_3-Epase_Enterobacteria
IPR036237 Xyl_isomerase-like_sf
IPR013022 Xyl_isomerase-like_TIM-brl
PfamiView protein in Pfam
PF01261 AP_endonuc_2, 1 hit
SUPFAMiSSF51658 SSF51658, 1 hit
TIGRFAMsiTIGR00542 hxl6Piso_put, 1 hit

Sequencei

Sequence statusi: Complete.

Q0SX88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKQIPLGI YEKALPAGEC WLERLRLAKT LGFDFVEMSV DETNERLSRL
60 70 80 90 100
DWSRVQRLAL VNAIVETGVR VPSMCLSAHR RFPLVSEDDA VRAQGLEIMR
110 120 130 140 150
KAIQFAQDVG IRVIQLSGYD VYYQEANNET RRRFRDGLKE SVEMASRAQV
160 170 180 190 200
TLAMEIMDYP LMNSISKALG YAHYLNNPWF QLYPDIGNLS AWDNDVQMEL
210 220 230 240 250
QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK QSGYCGPYLI
260 270 280
EMWSETAEDP AAEVVKACDW VKARMAKAGM VEAA
Length:284
Mass (Da):32,079
Last modified:September 5, 2006 - v1
Checksum:i4138EA24F37E0ACE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000266 Genomic DNA Translation: ABF06327.1

Genome annotation databases

EnsemblBacteriaiABF06327; ABF06327; SFV_4353
KEGGisfv:SFV_4353

Similar proteinsi

Entry informationi

Entry nameiULAE_SHIF8
AccessioniPrimary (citable) accession number: Q0SX88
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: March 28, 2018
This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
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Main funding by: National Institutes of Health