A0A8J8W6C7 · A0A8J8W6C7_9EURO
- ProteinBifunctional pyrimidine biosynthesis protein (PyrABCN)
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2250 (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 | 339 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 423 | |||||
Sequence: H | ||||||
Active site | 425 | |||||
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 > Penicillium
Accessions
- Primary accessionA0A8J8W6C7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MSQPASIQDSALPTSPTSGGVVGY | ||||||
Domain | 601-793 | ATP-grasp | ||||
Sequence: ARSMDSINEKCAKSASASTLEESLRVVKDIGFPVIVRAAYALGGLGSGFAENMDELKELCTKALAVSPQVLIERSMKGWKEIEYEVVRDAQDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSKEYCIIEVNARLSRSSALASKATGYPLAFIAAKLGL | ||||||
Domain | 1136-1327 | ATP-grasp | ||||
Sequence: SRMLDRIGVDQPAWKELTSIEEARTFCDKVGYPVLVRPSYVLSGAAMNTVYSEHDLANYLNQAADVSREHPVVITKYIENAKEIEMDAVARNGVMVGHFISEHVENAGVHSGDATLILPPQDLSPETVRRIEEATRKIGNALNVTGPYNIQFIAKDNDIKVIECNVRASRSFPFVSKVMGVDLIEMATKAMI | ||||||
Domain | 1393-1572 | MGS-like | ||||
Sequence: FKLPKRNILFSIGSYKEKLEMLPSIQKLHQLDYNLFATAGTADFLKEHGVPVKYLEILPGEDDDIKSEYSLTQHLSNNLIDLYINLPSSNRFRRPANYMSKGYRTRRMAVDYQTPLVTNVKNAKILIEAIARHYPLNIQTGDFQTSHRTVVLPGLINIAAFVPGLTTLGSKDFEQVTKAS | ||||||
Region | 1873-1903 | Disordered | ||||
Sequence: STHRIVPSSPVHKPTTPMVRPESALDRHTTP |
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
- Length2,250
- Mass (Da)246,917
- Last updated2022-05-25 v1
- Checksum32E92692FC14F39F
Keywords
- Technical term