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Protein

L-ribulose-5-phosphate 4-epimerase UlaF

Gene

ulaF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Pathwayi: L-ascorbate degradation

This protein is involved in step 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741ZincUniRule annotation
Metal bindingi93 – 931ZincUniRule annotation
Metal bindingi95 – 951ZincUniRule annotation
Metal bindingi167 – 1671ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:G7860-MONOMER.
ECOL316407:JW4156-MONOMER.
MetaCyc:G7860-MONOMER.
UniPathwayiUPA00263; UER00380.

Names & Taxonomyi

Protein namesi
Recommended name:
L-ribulose-5-phosphate 4-epimerase UlaFUniRule annotation (EC:5.1.3.4UniRule annotation)
Alternative name(s):
L-ascorbate utilization protein FUniRule annotation
Phosphoribulose isomeraseUniRule annotation
Gene namesi
Name:ulaFUniRule annotation
Synonyms:sgaE, yjfX
Ordered Locus Names:b4198, JW4156
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12498. ulaF.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228L-ribulose-5-phosphate 4-epimerase UlaFPRO_0000162921Add
BLAST

Proteomic databases

PaxDbiP39306.

Expressioni

Inductioni

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

Interactioni

Protein-protein interaction databases

BioGridi4262716. 6 interactions.
DIPiDIP-10868N.
IntActiP39306. 12 interactions.
MINTiMINT-1288465.
STRINGi511145.b4198.

Structurei

3D structure databases

ProteinModelPortaliP39306.
SMRiP39306. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldolase class II family. AraD/FucA subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107R0P. Bacteria.
COG0235. LUCA.
HOGENOMiHOG000218183.
InParanoidiP39306.
KOiK03077.
OMAiNPLHTPG.
OrthoDBiEOG6358F1.
PhylomeDBiP39306.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_01952. UlaF.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR023499. UlaF.
[Graphical view]
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 1 hit.

Sequencei

Sequence statusi: Complete.

P39306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKLKQQVFE ANMELPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM
60 70 80 90 100
KAADMVVVDM SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT
110 120 130 140 150
AWAQAGLAIP ALGTTHADYF FGDIPCTRGL SEEEVQGEYE LNTGKVIIET
160 170 180 190 200
LGNAEPLHTP GIVVYQHGPF AWGKDAHDAV HNAVVMEEVA KMAWIARGIN
210 220
PQLNHIDSFL MNKHFMRKHG PNAYYGQK
Length:228
Mass (Da):25,278
Last modified:February 1, 1995 - v1
Checksum:i3E96E7E0261E36B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97094.1.
U00096 Genomic DNA. Translation: AAC77155.1.
AP009048 Genomic DNA. Translation: BAE78199.1.
PIRiS56423.
RefSeqiNP_418619.1. NC_000913.3.
WP_001170847.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77155; AAC77155; b4198.
BAE78199; BAE78199; BAE78199.
GeneIDi948711.
KEGGiecj:JW4156.
eco:b4198.
PATRICi32123971. VBIEscCol129921_4330.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97094.1.
U00096 Genomic DNA. Translation: AAC77155.1.
AP009048 Genomic DNA. Translation: BAE78199.1.
PIRiS56423.
RefSeqiNP_418619.1. NC_000913.3.
WP_001170847.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP39306.
SMRiP39306. Positions 1-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262716. 6 interactions.
DIPiDIP-10868N.
IntActiP39306. 12 interactions.
MINTiMINT-1288465.
STRINGi511145.b4198.

Proteomic databases

PaxDbiP39306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77155; AAC77155; b4198.
BAE78199; BAE78199; BAE78199.
GeneIDi948711.
KEGGiecj:JW4156.
eco:b4198.
PATRICi32123971. VBIEscCol129921_4330.

Organism-specific databases

EchoBASEiEB2391.
EcoGeneiEG12498. ulaF.

Phylogenomic databases

eggNOGiENOG4107R0P. Bacteria.
COG0235. LUCA.
HOGENOMiHOG000218183.
InParanoidiP39306.
KOiK03077.
OMAiNPLHTPG.
OrthoDBiEOG6358F1.
PhylomeDBiP39306.

Enzyme and pathway databases

UniPathwayiUPA00263; UER00380.
BioCyciEcoCyc:G7860-MONOMER.
ECOL316407:JW4156-MONOMER.
MetaCyc:G7860-MONOMER.

Miscellaneous databases

PROiP39306.

Family and domain databases

Gene3Di3.40.225.10. 1 hit.
HAMAPiMF_01952. UlaF.
InterProiIPR001303. Aldolase_II/adducin_N.
IPR023499. UlaF.
[Graphical view]
PfamiPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTiSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMiSSF53639. SSF53639. 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, CHARACTERIZATION.
    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 nameiULAF_ECOLI
AccessioniPrimary (citable) accession number: P39306
Secondary accession number(s): Q2M6A7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 17, 2016
This is version 126 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.