HAMAP rule MF_01952
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_01952 |
| Accession | MF_01952 |
| Dates | 06-APR-2006 (Created)
07-MAY-2024 (Last updated, Version 25) |
| Name | UlaF |
| Scope(s) |
Bacteria Enterobacteriaceae |
| Template(s) | P39306; [ Recover all ] |
| Triggered by |
HAMAP; MF_01952 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ULAF |
| case <FTGroup:1> | |
| Protein name | RecName: Full=L-ribulose-5-phosphate 4-epimerase UlaF; EC=5.1.3.4; AltName: Full=L-ascorbate utilization protein F; AltName: Full=Phosphoribulose isomerase; |
| end case | |
| case not <FTGroup:1> | |
| Protein name | RecName: Full=Putative L-ribulose-5-phosphate 4-epimerase; |
| end case | |
| Gene name | Name=ulaF; |
Comments
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| FUNCTION | Catalyzes the isomerization of L-ribulose 5-phosphate to D- xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization. |
| CATALYTIC ACTIVITY | Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate; Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226; EC=5.1.3.4; |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; |
| PATHWAY | Cofactor degradation; L-ascorbate degradation; D-xylulose 5- phosphate from L-ascorbate: step 4/4. |
| INDUCTION | Induced by L-ascorbate. Repressed by UlaR. |
| SIMILARITY | Belongs to the aldolase class II family. AraD/FucA subfamily. |
Keywords
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Gene Ontology
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| GO:0008742; Molecular function:L-ribulose-phosphate 4-epimerase activity |
| GO:0008270; Molecular function:zinc ion binding |
| GO:0019854; Biological process:L-ascorbic acid catabolic process |
Cross-references
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| Pfam | PF00596; Aldolase_II; 1; |
Features
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| From: ULAF_ECOLI (P39306) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 26 | 27 | /ligand="substrate" | G-N | ||||||||
| BINDING | 43 | 44 | /ligand="substrate" | [TS]-G | ||||||||
| BINDING | 72 | 73 | /ligand="substrate" | S-S | ||||||||
| ACT_SITE | 118 | 118 | /note="Proton donor/acceptor" | D | ||||||||
| ACT_SITE | 225 | 225 | /note="Proton donor/acceptor" | Y | ||||||||
| BINDING | 74 | 74 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
D | 1 | |||||||
| BINDING | 93 | 93 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 95 | 95 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 167 | 167 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
Additional information
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| Size range | 228-228 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |