A0A8H7RBU1 · A0A8H7RBU1_9FUNG
- ProteinAspartate carbamoyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2249 (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 | 349 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 433 | |||||
Sequence: H | ||||||
Active site | 435 | |||||
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
- Recommended nameAspartate carbamoyltransferase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Mucoromycetes > Mucorales > Mucorineae > Mucoraceae > Mucor
Accessions
- Primary accessionA0A8H7RBU1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 609-801 | ATP-grasp | ||||
Sequence: AQALYEIDEKCAPSASAVTVEESITAANNIGYPVIVRAAYALGGLGSGFADNDKELIALCNKAFATSPQVLIEKSMKGWKEIEYEVVRDCQDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSKEYCIIEVNARLSRSSALASKATGYPLAFVAAKLGL | ||||||
Domain | 1146-1337 | ATP-grasp | ||||
Sequence: SRMCDNIGVDQPLWKELTSYEEAEVFCEKVGYPVLVRPSYVLSGAAMNVVSSKDDLESYLKEAAAVSRDYPVVISKYIEDAKEIEMDAVALDGKMIMHVVSEHVENAGVHSGDATLILPPQDLDPETVRKIEVATAKIGRALNITGPFNIQFIAKDNEIKVIECNVRAARSFPFVSKVTGIDLVEMATLAML | ||||||
Domain | 1403-1568 | MGS-like | ||||
Sequence: FSLPKKNILFSIGSYKEKIEMLPSVKRLHELGYSLFATTGTADFISEHGIPVKHLDTLDADTDDQIKAEYSLQQHLSNNMIDLYVNLPSRNRFRRPASYMSKGYRSRRMAVDYDIPLLTNVKCAKLFVEALARKKDFEILGIDFKSSSNTATLPGLFNINAFLPST | ||||||
Region | 1877-1900 | Disordered | ||||
Sequence: APKKKADSTPSDADISDVPETAPE |
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
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,249
- Mass (Da)247,335
- Last updated2022-01-19 v1
- Checksum0FBAEECDC4C285CF
Keywords
- Technical term