A0A1L9VWG1 · A0A1L9VWG1_ASPGL
- ProteinUncharacterized protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2252 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H+ + L-glutamate + phosphate
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 341 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 425 | |||||
Sequence: H | ||||||
Active site | 427 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | dihydroorotase activity | |
Molecular Function | metal ion binding | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | citrulline biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | UTP biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Aspergillus
Accessions
- Primary accessionA0A1L9VWG1
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 603-795 | ATP-grasp | ||||
Sequence: ARSMESINEKCAQSASASSLEEALEVVEQIKFPVIVRAAYALGGLGSGFADDMDQLKDLCIKAFAASPQVLIEKSMKGWKEIEYEVVRDAQDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSKEYCIIEVNARLSRSSALASKATGYPLAFIAAKLGL | ||||||
Domain | 1138-1329 | ATP-grasp | ||||
Sequence: SRMLDRIDVDQPAWKELTSIDEARGFCDAVGYPVLVRPSYVLSGAAMNTVYSEHDLASYLNQAADVSRDHPVVITKYIENAKEIEMDAVARNGVMVGHFISEHVENAGVHSGDATLILPPQDLSPETVRRIEEATSKIGNALNVTGPYNIQFIAKDNDIKVIECNVRASRSFPFVSKVMGVDLIEMATKAMI | ||||||
Domain | 1395-1547 | MGS-like | ||||
Sequence: FRLPKRNILFSIGSYKEKLEMLPSIQKLHQNGFNLFATAGTADFLKENGVPVKYLEILPGQEEDIKTEYSLTQHLANNLIDLYINLPSNNRFRRPANYMSKGYRTRRMAVDYQTPLVTNVKNAKILIEAIARHFPLNIQTSDYQTSHRSIVLP | ||||||
Region | 1867-1920 | Disordered | ||||
Sequence: KGTDMSGHRIAPTSPVVKPLSPLVQPRSESSLDRRLSLSGTPGRGLRRGLDQAG |
Sequence similarities
In the 2nd section; belongs to the CarB family.
In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
In the N-terminal section; belongs to the CarA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,252
- Mass (Da)247,106
- Last updated2017-03-15 v1
- ChecksumD3B7E078F9C9B2D0
Keywords
- Technical term