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Q8FAI6 (ULAF_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-ribulose-5-phosphate 4-epimerase UlaF

EC=5.1.3.4
Alternative name(s):
L-ascorbate utilization protein F
Phosphoribulose isomerase
Gene names
Name:ulaF
Ordered Locus Names:c5288
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization By similarity. HAMAP MF_01952

Catalytic activity

L-ribulose 5-phosphate = D-xylulose 5-phosphate. HAMAP MF_01952

Cofactor

Binds 1 zinc ion per subunit Potential.

Pathway

Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 4/4. HAMAP MF_01952

Induction

Induced by L-ascorbate. Repressed by UlaR By similarity. HAMAP MF_01952

Sequence similarities

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

Sequence caution

The sequence AAN83709.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionL-ribulose-phosphate 4-epimerase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228L-ribulose-5-phosphate 4-epimerase UlaF HAMAP MF_01952
PRO_0000233243

Sites

Metal binding741Zinc By similarity
Metal binding931Zinc By similarity
Metal binding951Zinc By similarity
Metal binding1671Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FAI6 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 449842FBFAAAE632

FASTA22825,339
        10         20         30         40         50         60 
MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM 

        70         80         90        100        110        120 
SGKVVEGEYR PSSDTATHLE LYRRYPSLGG IVHTHSTHAT AWAQAGLAIP ALGTTHADYF 

       130        140        150        160        170        180 
FGDIPCTRGL SEEEVQGEYE LNTGKVIIET LGDAEPLHTP GIVVYQHGPF AWGKDAHDAV 

       190        200        210        220 
HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN83709.1. Different initiation.
RefSeqNP_757135.2. NC_004431.1.

3D structure databases

ProteinModelPortalQ8FAI6.
SMRQ8FAI6. Positions 1-219.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000044709; EBESCP00000043058; EBESCG00000043759.
GeneID1037452.
GenomeReviewsGene locus c5288 in contig AE014075_GR.
KEGGecc:c5288.
NMPDRfig|199310.1.peg.5178.
PATRIC18288223. VBIEscCol75197_4953.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009319.
HOGENOMHBG541069.
OMAIDSYLMN.
ProtClustDBPRK12348.

Family and domain databases

HAMAPMF_01952. UlaF.
[Tree]
InterProIPR001303. Aldolase_II/adducin_N.
IPR023499. UlaF.
[Graphical view]
Gene3DG3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
KOK03077.
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMSSF53639. Aldolase_II_N. 1 hit.
ProtoNetSearch...

Entry information

Entry nameULAF_ECOL6
AccessionPrimary (citable) accession number: Q8FAI6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: January 25, 2012
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families