A0A6C7HVC5 · A0A6C7HVC5_SALEP
- ProteinL-ribulose-5-phosphate 4-epimerase UlaF
- GenesgaE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids228 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization.
Catalytic activity
- L-ribulose 5-phosphate = D-xylulose 5-phosphate
Cofactor
Note: Binds 1 zinc ion per subunit.
Pathway
Cofactor degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 4/4.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26-27 | substrate | ||||
Sequence: GN | ||||||
Binding site | 43-44 | substrate | ||||
Sequence: SG | ||||||
Binding site | 72-73 | substrate | ||||
Sequence: SS | ||||||
Binding site | 74 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 93 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 95 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 118 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 167 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 225 | Proton donor/acceptor | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | L-ribulose-phosphate 4-epimerase activity | |
Molecular Function | zinc ion binding | |
Biological Process | L-ascorbic acid catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-ribulose-5-phosphate 4-epimerase UlaF
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionA0A6C7HVC5
Proteomes
Expression
Induction
Induced by L-ascorbate. Repressed by UlaR.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-194 | Class II aldolase/adducin N-terminal | ||||
Sequence: QQVFDANMDLPRYGLVTFTWGNVSAIDRERGLVVIKPSGVAYETMKVDDMVVVDMDGKVVEGGYRPSSDTATHLALYQRYPSLGGVVHTHSTHATAWAQAGMAIPALGTTHADYFFGDIPCTRALSEEEVQGEYELNTGKVIIETLGEVEPLHTPGIVVYQHGPFAWGKDAHDAVHNAVVMEEVARMAW |
Sequence similarities
Belongs to the aldolase class II family. AraD/FucA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length228
- Mass (Da)25,214
- Last updated2020-06-17 v1
- ChecksumBA9E5BB7153E481E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AM933172 EMBL· GenBank· DDBJ | CAR35714.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAQLS010000014 EMBL· GenBank· DDBJ | HAD9861804.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAQPD010000010 EMBL· GenBank· DDBJ | HAE0281100.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAQPM010000010 EMBL· GenBank· DDBJ | HAE0331358.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAQRD010000014 EMBL· GenBank· DDBJ | HAE0519554.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DAAQSA010000010 EMBL· GenBank· DDBJ | HAE0638776.1 EMBL· GenBank· DDBJ | Genomic DNA |