S9QW30 · S9QW30_9RHOB
- ProteinMultifunctional fusion protein
- GenenadA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1413 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic activity
- ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; quinolinate from iminoaspartate: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 667 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 1131 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1149 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 1194 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1220-1222 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: YVN | ||||||
Binding site | 1237 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 1279 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1305-1307 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: HPE | ||||||
Binding site | 1322 | iminosuccinate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 1365 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | aminoacyl-tRNA editing activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | quinolinate synthetase A activity | |
Molecular Function | valine-tRNA ligase activity | |
Biological Process | NAD biosynthetic process | |
Biological Process | valyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameValine--tRNA ligase
- EC number
- Alternative names
- Recommended nameQuinolinate synthase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Rubellimicrobium
Accessions
- Primary accessionS9QW30
Proteomes
Subcellular Location
Interaction
Family & Domains
Features
Showing features for domain, motif, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-483 | Aminoacyl-tRNA synthetase class Ia | ||||
Sequence: ALWEEAGAFRAGVNARPGAEAFSVVLPPPNVTGSLHMGHAFNATLQDILVRWHRMKGHDVLWQPGTDHAGIATQMVVERELAKQGRRRTDFTREAFVDLVWQQKARSGGAIRAQLDRLGASCDWSREAFTMDPSFQEAVLEVFVRWYEEGLIFRGQRLVNWDPHFETAISDLEVENREIQGHMWHFRYPLAGGETYLHVERDAEGRILLEEERDWIAIATTRPETMLGDGAVAVHPSDARYAPIIGKLCEIPVGPKGQRRLIPIIADDYPDPAFGSGAVKITGAHDFNDYKVAQRHGLPLYRLMDTKGRMRSDGLPYEDSVAIAVAIARGERPAGDVSQVNLVPEEMRGLDRFEARRLIVSQIEAEGLSVMTDSADGPVPLVESKVIMQPFGDRSGVVIEPMLTDQWFVDTARIVRPAIDAVREGRTAILPERDAKVYFNWLENIEPWCISRQLWWGHRIPVWYGF | ||||||
Motif | 46-56 | 'HIGH' region | ||||
Sequence: PNVTGSLHMGH | ||||||
Domain | 583-704 | Aminoacyl-tRNA synthetase class Ia | ||||
Sequence: WRDPDVLDTWFSSGIWPIGTLGWPADTPALRRYYPTSVLVTGFDIIFFWVARMMMMQLALVGEVPFRTVYVHALVRDEKGRKMSKSVGNVIDPIELIDEYGADAVRFTLAAMAAMGRDLRLS | ||||||
Motif | 664-668 | 'KMSKS' region | ||||
Sequence: KMSKS | ||||||
Domain | 747-894 | Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase anticodon-binding | ||||
Sequence: NRWILGETARAAEAVEAALGAFRFDEAARALHAFVWGVVCDWYVEFSKPLLGGGDAALKAETQAVMGWVLDRCLILMHPFMPFVTETLWQQTGPREGLLAHAEWPDLRAVDLVDPAAEAEMRWTVALIEGIRSVRAQMNVPAGLTVPV | ||||||
Domain | 951-1016 | Valyl-tRNA synthetase tRNA-binding arm | ||||
Sequence: DIAAETARMQKALRKAETEAAALRGRLGNPGFLASAPEEVVEETRGSLAAREAEIEQIRSALARLA | ||||||
Coiled coil | 956-1018 | |||||
Sequence: TARMQKALRKAETEAAALRGRLGNPGFLASAPEEVVEETRGSLAAREAEIEQIRSALARLAEA | ||||||
Region | 1027-1063 | Disordered | ||||
Sequence: AAVHADLQSPRRGDRKPALGEGRARATRPVTGAEGGP | ||||||
Compositional bias | 1034-1048 | Basic and acidic residues | ||||
Sequence: QSPRRGDRKPALGEG |
Domain
The C-terminal coiled-coil domain is crucial for aminoacylation activity.
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site.
Sequence similarities
Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily.
Belongs to the quinolinate synthase family. Type 2 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,413
- Mass (Da)156,444
- Last updated2013-10-16 v1
- Checksum7E0113E314FE0A90
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1034-1048 | Basic and acidic residues | ||||
Sequence: QSPRRGDRKPALGEG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AOLV01000029 EMBL· GenBank· DDBJ | EPX83787.1 EMBL· GenBank· DDBJ | Genomic DNA |