A0A9Q5I2D2 · A0A9Q5I2D2_SANBA
- ProteinGlutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1873 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic activity
- ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H+ + L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 72 | Charge relay system | ||||
Sequence: K | ||||||
Active site | 157 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 181 | Acyl-ester intermediate | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | glutamyl-tRNA(Gln) amidotransferase complex | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Cellular Component | VCP-NPL4-UFD1 AAA ATPase complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | |
Molecular Function | O-acyltransferase activity | |
Molecular Function | polyubiquitin modification-dependent protein binding | |
Biological Process | autophagosome maturation | |
Biological Process | glutaminyl-tRNAGln biosynthesis via transamidation | |
Biological Process | mitochondrial translation | |
Biological Process | mitotic spindle disassembly | |
Biological Process | retrograde protein transport, ER to cytosol |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial
- EC number
- Short namesGlu-AdT subunit A
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Hymenochaetales > Hymenochaetaceae > Sanghuangporus
Accessions
- Primary accessionA0A9Q5I2D2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1588-1619 | Helical | ||||
Sequence: LLMPICLFVFFFACSFPPLWPAAALYMIWVYY |
Keywords
- Cellular component
Interaction
Subunit
Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A, B and C subunits.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 141-160 | Disordered | ||||
Sequence: LSSQSEIERERRSAGGSSGG | ||||||
Region | 500-545 | Disordered | ||||
Sequence: VDHRQRSNMADPSGAPPQPGPDDTSTAILRPKKSPNRLLVDDTTND | ||||||
Domain | 536-621 | CDC48 N-terminal subdomain | ||||
Sequence: RLLVDDTTNDDNSVCTLHPATMERLGLFRGDTVLVRGKKRRDTVLICLASEDGSVEEGKIQMNKVARNNLRVKLADLVHISPLPDI | ||||||
Domain | 638-704 | CDC48 | ||||
Sequence: GLSGNLFEVYLKPYFLEAYRPVRKGDTFKVRGGMREVEFKVIETDPAEYCIVAQDTVIHTGTHSFTQ | ||||||
Domain | 664-739 | CDC48 N-terminal subdomain | ||||
Sequence: TFKVRGGMREVEFKVIETDPAEYCIVAQDTVIHTGTHSFTQXGSVEEGKIQMNKVARNNLRVKLADLVHIAPLPDI | ||||||
Domain | 756-822 | CDC48 | ||||
Sequence: GLSGNLFEVYLKPYFLEAYRPVRKGDTFKVRGGMREVEFKVIETDPAEYCIVAQDTVIHTEGDPVKR | ||||||
Domain | 868-1004 | AAA+ ATPase | ||||
Sequence: PPRGILMYGPPGTGKTLMARAVANETGAFFFLINGPEIMSKMAGESESNLRKAFEEAEKNSPSIIFIDEIDSIAPKREKTNGEVERRVVSQLLTLMDGLKARSNVVVMAATNRPNSIDPALRRFGRFDREVDIGIPD | ||||||
Domain | 1141-1281 | AAA+ ATPase | ||||
Sequence: PSKGVLFYGPPGTGKTLLAKAIANECQANFISIKGPELLTMWFGESEANVRDVFDKARAAAPCVMFFDELDSIAKARGSSMGGDAGGAGDRVLNQLLTEMDGMNAKKNVFIIGATNRPDQIDPALLRPGRLDQLIYIPLPD | ||||||
Region | 1403-1492 | Disordered | ||||
Sequence: GSSFRFPEGEPSASGGAAASSGNAAFGEDAQDDDFDMAETEYVLKQRRGTGTATGAGTSSSASSGTGTSTSVPEDHHPKIHISSQDCDDD | ||||||
Compositional bias | 1453-1475 | Polar residues | ||||
Sequence: GTATGAGTSSSASSGTGTSTSVP | ||||||
Compositional bias | 1476-1492 | Basic and acidic residues | ||||
Sequence: EDHHPKIHISSQDCDDD |
Sequence similarities
Belongs to the amidase family. GatA subfamily.
Belongs to the diacylglycerol acyltransferase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,873
- Mass (Da)205,602
- Last updated2023-09-13 v1
- Checksum347BFF941E4D019E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1453-1475 | Polar residues | ||||
Sequence: GTATGAGTSSSASSGTGTSTSVP | ||||||
Compositional bias | 1476-1492 | Basic and acidic residues | ||||
Sequence: EDHHPKIHISSQDCDDD |
Keywords
- Technical term