O68195 · DDRA_KLEM8
- ProteinDiol dehydratase-reactivating factor large subunit
- GeneddrA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids610 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Large subunit of the diol dehydratase-reactivating factor (DDR), which reactivates suicidally inhibited adenosylcobalamin-dependent diol dehydratase (DD, pddA, pddB, pddC). DDR acts as a chaperone, reactivating inactivated DD holoenzyme in the presence of ATP, Mg2+ and free adenosylcobalamin (AdoCbl), by mediating the exchange of the tightly bound damaged cofactor AdoCbl for a free intact one (PubMed:10529189, PubMed:17916188, PubMed:18586770, PubMed:21040475, PubMed:9405397, PubMed:9920879).
Reactivation takes place in two steps: ADP-dependent cobalamin release, then ATP-dependent dissociation of the DD apoenzyme-DDR complex. DDR has weak ATPase activity which is required for DD reactivation (PubMed:10529189, PubMed:17916188, PubMed:21040475).
This subunit contains the adenosine nucleotide binding site (PubMed:16338403).
Activates glycerol-inactivated, O2-inactivated holoenzyme and inactivated enzyme-cyanocobalamin complex (PubMed:9920879).
Also reactivates glycerol-inactivated hologlycerol dehydratase, a DD isozyme (PubMed:17916188).
Reactivation takes place in two steps: ADP-dependent cobalamin release, then ATP-dependent dissociation of the DD apoenzyme-DDR complex. DDR has weak ATPase activity which is required for DD reactivation (PubMed:10529189, PubMed:17916188, PubMed:21040475).
This subunit contains the adenosine nucleotide binding site (PubMed:16338403).
Activates glycerol-inactivated, O2-inactivated holoenzyme and inactivated enzyme-cyanocobalamin complex (PubMed:9920879).
Also reactivates glycerol-inactivated hologlycerol dehydratase, a DD isozyme (PubMed:17916188).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
6.9 mM | ATP, during activation and reactivation of glycerol-inactivated holoenzyme or enzyme-CN-Cbl complex |
kcat for enzyme-bound damaged AdoCbl is 0.14 min-1, kcat for reactivation of CN-Cbl-inactivated enzyme is 0.27 min-1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 11-13 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NSS | ||||||
Binding site | 105 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 166 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 183 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 459-462 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EEIK | ||||||
Binding site | 557-558 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 591 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | hydrolase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameDiol dehydratase-reactivating factor large subunit
- Short namesDDR large subunit
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Klebsiella/Raoultella group > Klebsiella
Accessions
- Primary accessionO68195
- Secondary accessions
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000412975 | 1-610 | Diol dehydratase-reactivating factor large subunit | |||
Sequence: MRYIAGIDIGNSSTEVALATLDEAGALTITHSALAETTGIKGTLRNVFGIQEALALVARGAGIAVSDISLIRINEATPVIGDVAMETITETIITESTMIGHNPKTPGGAGLGTGITITPQELLTRPADAPYILVVSSAFDFADIASVINASLRAGYQITGVILQRDDGVLVSNRLEKPLPIVDEVLYIDRIPLGMLAAIEVAVPGKVIETLSNPYGIATVFNLSPEETKNIVPMARALIGNRSAVVVKTPSGDVKARAIPAGNLELLAQGRSVRVDVAAGAEAIMKAVDGCGRLDNVTGESGTNIGGMLEHVRQTMAELTNKPSSEIFIQDLLAVDTSVPVSVTGGLAGEFSLEQAVGIASMVKSDRLQMAMIAREIEQKLNIDVQIGGAEAEAAILGALTTPGTTRPLAILDLGAGSTDASIINPKGDIIATHLAGAGDMVTMIIARELGLEDRYLAEEIKKYPLAKVESLFHLRHEDGSVQFFSTPLPPAVFARVCVVKADELVPLPGDLALEKVRAIRRSAKERVFVTNALRALRQVSPTGNIRDIPFVVLVGGSSLDFEVPQLVTDALAHYRLVAGRGNIRGSEGPRNAVATGLILSWHKEFAHER |
Interaction
Subunit
Component of the DDR complex, a heterotetramer of DdrA2/DdrB2 (Probable) (PubMed:10529189, PubMed:16338403, PubMed:17916188, PubMed:21040475, PubMed:9920879).
The DDR complex interacts with the diol dehydratase complex in the presence of ADP but not ATP (PubMed:10529189, PubMed:21040475).
The DDR complex interacts with the diol dehydratase complex in the presence of ADP but not ATP (PubMed:10529189, PubMed:21040475).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O68195 | ddrB O68196 | 4 | EBI-8491873, EBI-8491890 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length610
- Mass (Da)64,267
- Last updated1998-08-01 v1
- ChecksumB14C6DCBE13FA138
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF017781 EMBL· GenBank· DDBJ | AAC15871.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP003218 EMBL· GenBank· DDBJ | AEX02039.1 EMBL· GenBank· DDBJ | Genomic DNA |