A0A2G6LB29 · A0A2G6LB29_9GAMM
- ProteinMultifunctional fusion protein
- Genetal
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1182 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic activity
- D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Mg2+ ion per subunit.
Note: Binds 2 Zn2+ ions per homotetramer.
Pathway
Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 304 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 347 | Mg2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 405 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Binding site | 408 | Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: C | ||||||
Active site | 957 | Schiff-base intermediate with substrate | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic side of plasma membrane | |
Molecular Function | magnesium ion binding | |
Molecular Function | ribonuclease E activity | |
Molecular Function | RNA endonuclease activity | |
Molecular Function | rRNA binding | |
Molecular Function | transaldolase activity | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | mRNA catabolic process | |
Biological Process | pentose-phosphate shunt | |
Biological Process | rRNA processing | |
Biological Process | tRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameRibonuclease E
- EC number
- Short namesRNase E
- Recommended nameTransaldolase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria
Accessions
- Primary accessionA0A2G6LB29
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Keywords
- Cellular component
Interaction
Subunit
Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, RNase E assembles into a homotetramer formed by a dimer of dimers.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-121 | S1 motif | ||||
Sequence: ANIYKGKITRVEPSLEAAFVDYGADRHGFLPIKEISKDYFSGSTAVGKNGRPDYKKLIREGQAVMVQVEKEERGNKGAALTTY | ||||||
Region | 405-408 | Required for zinc-mediated homotetramerization and catalytic activity | ||||
Sequence: CPRC | ||||||
Region | 568-761 | Disordered | ||||
Sequence: TKKMKTAKTEDDAGKKADKADKEKYSRGEGHKKNGQRNRKKERPSGKNNKVSDGRKNTNKTIDKKTGKTTSNKKPPTEKQVKKTGSRNGHGKSGQSNQPVERTNKVDKADKTNKADKKVAKPFVNPYAKDKEKIRQGRPVSEDAIRGAGKADFAKQPDKASAQQVESTQENQKTKRPTTKDEGRKKAKKNYPDK | ||||||
Compositional bias | 571-599 | Basic and acidic residues | ||||
Sequence: MKTAKTEDDAGKKADKADKEKYSRGEGHK | ||||||
Compositional bias | 608-652 | Basic and acidic residues | ||||
Sequence: KERPSGKNNKVSDGRKNTNKTIDKKTGKTTSNKKPPTEKQVKKTG | ||||||
Compositional bias | 654-669 | Polar residues | ||||
Sequence: RNGHGKSGQSNQPVER | ||||||
Compositional bias | 670-707 | Basic and acidic residues | ||||
Sequence: TNKVDKADKTNKADKKVAKPFVNPYAKDKEKIRQGRPV | ||||||
Compositional bias | 740-761 | Basic and acidic residues | ||||
Sequence: KTKRPTTKDEGRKKAKKNYPDK |
Sequence similarities
Belongs to the RNase E/G family. RNase E subfamily.
Belongs to the RNase E/G family. RNase G subfamily.
Belongs to the transaldolase family. Type 2 subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,182
- Mass (Da)132,053
- Last updated2018-01-31 v1
- Checksum2F26D02E3AFAF374
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 571-599 | Basic and acidic residues | ||||
Sequence: MKTAKTEDDAGKKADKADKEKYSRGEGHK | ||||||
Compositional bias | 608-652 | Basic and acidic residues | ||||
Sequence: KERPSGKNNKVSDGRKNTNKTIDKKTGKTTSNKKPPTEKQVKKTG | ||||||
Compositional bias | 654-669 | Polar residues | ||||
Sequence: RNGHGKSGQSNQPVER | ||||||
Compositional bias | 670-707 | Basic and acidic residues | ||||
Sequence: TNKVDKADKTNKADKKVAKPFVNPYAKDKEKIRQGRPV | ||||||
Compositional bias | 740-761 | Basic and acidic residues | ||||
Sequence: KTKRPTTKDEGRKKAKKNYPDK |