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B1IT08 (ULAF_ECOLC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:EcolC_3815
OrganismEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) [Complete proteome] [HAMAP]
Taxonomic identifier481805 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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.

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_1000088485

Sites

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

Sequences

Sequence LengthMass (Da)Tools
B1IT08 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 06D867A89F9E6B4A

FASTA22825,280
        10         20         30         40         50         60 
MQKLKQQVFE ANMELPRYGL ATFTWGNVSA IDRERGLVVI KPSGVAYETM KAADMVVVDM 

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

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

       190        200        210        220 
HNAVVMEEVA KMAWIARSIN PQLNHIDSFL MNKHFMRKHG PNAYYGQK

« Hide

References

[1]"Complete sequence of Escherichia coli C str. ATCC 8739."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8739 / DSM 1576 / Crooks.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000946 Genomic DNA. Translation: ACA79419.1.
RefSeqYP_001726746.1. NC_010468.1.

3D structure databases

ProteinModelPortalB1IT08.
SMRB1IT08. Positions 1-219.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1IT08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000007355; EBESCP00000007039; EBESCG00000006418.
GeneID6064755.
GenomeReviewsGene locus EcolC_3815 in contig CP000946_GR.
KEGGecl:EcolC_3815.
PATRIC18230789. VBIEscCol82905_4084.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000009319.
HOGENOMHBG541069.
OMAIDSYLMN.
ProtClustDBPRK12348.

Enzyme and pathway databases

BioCycECOL481805:ECOLC_3815-MONOMER.

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_ECOLC
AccessionPrimary (citable) accession number: B1IT08
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 28 of the entry and version 1 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

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