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Protein

L-ribulose-5-phosphate 3-epimerase UlaE

Gene

ulaE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization.UniRule annotation1 Publication

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 (ulaG)
  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

  • L-ascorbic acid catabolic process Source: UniProtKB-UniPathway
  • L-ascorbic acid metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciEcoCyc:G7859-MONOMER.
ECOL316407:JW4155-MONOMER.
MetaCyc:G7859-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
Synonyms:sgaU, yjfW
Ordered Locus Names:b4197, JW4155
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12497. ulaE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 284284L-ribulose-5-phosphate 3-epimerase UlaEPRO_0000097716Add
BLAST

Proteomic databases

PaxDbiP39305.
PRIDEiP39305.

Expressioni

Inductioni

Induced by L-ascorbate. Repressed by UlaR.UniRule annotation2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4262715. 7 interactions.
IntActiP39305. 1 interaction.
STRINGi511145.b4197.

Structurei

3D structure databases

ProteinModelPortaliP39305.
SMRiP39305. Positions 5-280.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG41064BZ. Bacteria.
COG3623. LUCA.
HOGENOMiHOG000126090.
InParanoidiP39305.
KOiK03079.
OMAiQAGMGHI.
OrthoDBiEOG6FFS58.
PhylomeDBiP39305.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_01951. UlaE.
InterProiIPR004560. L-Ru-5P_3-Epase.
IPR023492. L-Ru-5P_3-Epase_Enterobacteria.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR00542. hxl6Piso_put. 1 hit.

Sequencei

Sequence statusi: Complete.

P39305-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSKQIPLGI YEKALPAGEC WLERLQLAKT LGFDFVEMSV DETDDRLSRL
60 70 80 90 100
NWSREQRLAL VNAIVETGVR VPSMCLSAHR RFPLGSEDDA VRAQGLEIMR
110 120 130 140 150
KAIQFAQDVG IRVIQLAGYD VYYQEANNET RRRFRDGLKE SVEMASRAQV
160 170 180 190 200
TLAMEIMDYP LMSSISKALG YAHYLNNPWF QLYPDIGNLS AWDNDVQMEL
210 220 230 240 250
QAGIGHIVAV HVKDTKPGVF KNVPFGEGVV DFERCFETLK QSGYCGPYLI
260 270 280
EMWSETAEDP AAEVAKARDW VKARMAKAGM VEAA
Length:284
Mass (Da):32,007
Last modified:February 1, 1995 - v1
Checksum:iAAA9F000B9D94A08
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97093.1.
U00096 Genomic DNA. Translation: AAC77154.1.
AP009048 Genomic DNA. Translation: BAE78198.1.
PIRiS56422.
RefSeqiNP_418618.1. NC_000913.3.
WP_000949502.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77154; AAC77154; b4197.
BAE78198; BAE78198; BAE78198.
GeneIDi948712.
KEGGiecj:JW4155.
eco:b4197.
PATRICi32123969. VBIEscCol129921_4329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97093.1.
U00096 Genomic DNA. Translation: AAC77154.1.
AP009048 Genomic DNA. Translation: BAE78198.1.
PIRiS56422.
RefSeqiNP_418618.1. NC_000913.3.
WP_000949502.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP39305.
SMRiP39305. Positions 5-280.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262715. 7 interactions.
IntActiP39305. 1 interaction.
STRINGi511145.b4197.

Proteomic databases

PaxDbiP39305.
PRIDEiP39305.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77154; AAC77154; b4197.
BAE78198; BAE78198; BAE78198.
GeneIDi948712.
KEGGiecj:JW4155.
eco:b4197.
PATRICi32123969. VBIEscCol129921_4329.

Organism-specific databases

EchoBASEiEB2390.
EcoGeneiEG12497. ulaE.

Phylogenomic databases

eggNOGiENOG41064BZ. Bacteria.
COG3623. LUCA.
HOGENOMiHOG000126090.
InParanoidiP39305.
KOiK03079.
OMAiQAGMGHI.
OrthoDBiEOG6FFS58.
PhylomeDBiP39305.

Enzyme and pathway databases

UniPathwayiUPA00263; UER00379.
BioCyciEcoCyc:G7859-MONOMER.
ECOL316407:JW4155-MONOMER.
MetaCyc:G7859-MONOMER.

Miscellaneous databases

PROiP39305.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_01951. UlaE.
InterProiIPR004560. L-Ru-5P_3-Epase.
IPR023492. L-Ru-5P_3-Epase_Enterobacteria.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR00542. hxl6Piso_put. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Novel phosphotransferases system genes revealed by bacterial genome analysis: operons encoding homologues of sugar-specific permease domains of the phosphotransferase system and pentose catabolic enzymes."
    Reizer J., Charbit A., Reizer A., Saier M.H. Jr.
    Genome Sci. Technol. 1:53-75(1996)
    Cited for: DISCUSSION OF SEQUENCE.
  5. "Utilization of L-ascorbate by Escherichia coli K-12: assignments of functions to products of the yjf-sga and yia-sgb operons."
    Yew W.S., Gerlt J.A.
    J. Bacteriol. 184:302-306(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "The gene yjfQ encodes the repressor of the yjfR-X regulon (ula), which is involved in L-ascorbate metabolism in Escherichia coli."
    Campos E., Aguilar J., Baldoma L., Badia J.
    J. Bacteriol. 184:6065-6068(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.
  7. "Regulation of expression of the divergent ulaG and ulaABCDEF operons involved in L-ascorbate dissimilation in Escherichia coli."
    Campos E., Baldoma L., Aguilar J., Badia J.
    J. Bacteriol. 186:1720-1728(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSCRIPTIONAL REGULATION.

Entry informationi

Entry nameiULAE_ECOLI
AccessioniPrimary (citable) accession number: P39305
Secondary accession number(s): Q2M6A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.