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Reviewed, UniProtKB/Swiss-Prot Q8ZK85 (ULAF_SALTY)

Last modified November 3, 2009. Version 42. 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:
    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: STM4388
OrganismSalmonella typhimurium [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

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

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.

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)
   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 – 228228L-ribulose-5-phosphate 4-epimerase ulaF HAMAP MF_01952
PRO_0000233247

Sites

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

Sequences

Sequence LengthMass (Da)Tools
Q8ZK85-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 16399B00A84E55A8

FASTA22825,327
        10         20         30         40         50         60 
MQKLKQQVFD ANMDLPRYGL VTFTWGNVSA IDRERGLVVI KPSGVAYETM KVDDMVVVDM 

        70         80         90        100        110        120 
DGKVVEGRYR PSSDTATHLA LYQRYPSLGG VVHTHSTHAT AWAQAGMAIP ALGTTHADYF 

       130        140        150        160        170        180 
FGDIPCTRAL SEEEVQGEYE LNTGKVIIET LGEVEPLHTP GIVVYQHGPF AWGKDAHDAV 

       190        200        210        220 
HNAVVMEEVA RMAWIARGIN PALNPIDDYL MNKHFMRKHG PNAYYGQK 

« Hide

Cross-references

Sequence databases

AE006468 Genomic DNA. Translation: AAL23208.1.
RefSeqNP_463249.1.

3D structure databases

HSSPHSSP built from PDB template 1K0W based on UniProtKB P08203.
ModBaseSearch...

Genome annotation databases

GeneID1255914.
GenomeReviewsGene locus STM4388 in contig AE006468_GR.
KEGGstm:STM4388.
NMPDRfig|99287.1.peg.4222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8ZK85.
OMADAEPLHT.

Enzyme and pathway databases

BioCycSTYP99287:STM4388-MON.
BRENDA5.1.3.4. 2.

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_SALTY
AccessionPrimary (citable) accession number: Q8ZK85
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: March 1, 2002
Last modified: November 3, 2009
This is version 42 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