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Reviewed, UniProtKB/Swiss-Prot P0C1B9 (ULAF_SHIBS)

Last modified April 14, 2009. Version 20. 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:
    Putative L-ribulose-5-phosphate 4-epimerase ulaF
    EC=5.1.3.4
Alternative name(s):
    Phosphoribulose isomerase
    L-ascorbate utilization protein F
Gene names
Name: ulaF
Ordered Locus Names: SBO_4257
OrganismShigella boydii serotype 4 (strain Sb227) [Complete proteome] [HAMAP]
Taxonomic identifier300268 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceUncertain.

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.

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

Induction

Induced by L-ascorbate. Repressed by ulaR By similarity.

Sequence similarities

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

Caution

Could be the product of a pseudogene.

Sequence caution

The sequence CP000036 differs from that shown. Reason: Erroneous termination at position 172. Translated as Trp.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processL-ascorbic acid metabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionL-ribulose-phosphate 4-epimerase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228Putative L-ribulose-5-phosphate 4-epimerase ulaF HAMAP MF_01952
PRO_0000234033

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P0C1B9-1 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 978176AF708AEE90

FASTA22825,338
        10         20         30         40         50         60 
MQKLKQQVFE ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KADDMVVVDM 

        70         80         90        100        110        120 
SGKVVEGKYR 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]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000036 Genomic DNA. No translation available.

3D structure databases

ModBaseSearch...

Genome annotation databases

GenomeReviewsGene locus SBO_4257 in contig CP000036_GR.
KEGGsbo:SBO_4257.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0C1B9.

Family and domain databases

HAMAPMF_01952.
[Tree]
InterProIPR001303. Aldolase_II/adducin_N.
[Graphical view]
Gene3DG3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameULAF_SHIBS
AccessionPrimary (citable) accession number: P0C1B9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: April 14, 2009
This is version 20 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