A0A1C5ESV9 · A0A1C5ESV9_9ACTN
- ProteinMultifunctional fusion protein
- GenepyrC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids755 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
Catalytic activity
- (S)-dihydroorotate + H2O = H+ + N-carbamoyl-L-aspartate
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 55 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 56 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 83 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 105 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 135 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 138 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 176 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 230 | L-aspartate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 271 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 272 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 383 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 385 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 385-387 | substrate | ||||
Sequence: HLR | ||||||
Binding site | 417 | substrate | ||||
Sequence: N | ||||||
Binding site | 477 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 477 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 504 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 557 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 603 | substrate | ||||
Sequence: N | ||||||
Active site | 630 | |||||
Sequence: D | ||||||
Binding site | 630 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 634 | substrate | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Molecular Function | dihydroorotase activity | |
Molecular Function | zinc ion binding | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | amino acid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameAspartate carbamoyltransferase
- EC number
- Alternative names
- Recommended nameDihydroorotase
- EC number
- Short namesDHOase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A1C5ESV9
Proteomes
Interaction
Subunit
Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-147 | Aspartate/ornithine carbamoyltransferase carbamoyl-P binding | ||||
Sequence: RHLISAADLSRDDAVLILDTAEEMARVADRPIKKLPTLRGRTVVNLFFEDSTRTRISFEAAEKRLSADVINFSAKGSSVSKGESLKDTAQTLEAMGVDAVVIRHGASGAPYRLATSGWIDAAVINAGDGTHQHPTQALLDAFTMR | ||||||
Domain | 163-309 | Aspartate/ornithine carbamoyltransferase Asp/Orn-binding | ||||
Sequence: GKRVTLVGDVLHSRVARSNVDLLHTLGAEVTLVAPPTLIPVGVESWPCEVSYDLDSTLPKCDAVMMLRVQRERMNAAFFPTEREYSRRYGLDGDRMAKLPEHAIVMHPGPMVRGMEITAEVADSDRCTAVEQVANGVSIRMAVLYLL | ||||||
Domain | 374-747 | Amidohydrolase-related | ||||
Sequence: VLLPGLVDLHTHLREPGREDSETVLTGTRAAASGGYTAVFAMANTFPVADTAGVVEQVWRLGKEHGYCDVQPIGAVTVGLEGRKLAELGAMHESAAGVTVFSDDGKCVDDAVIMRRALEYVKAFGGIVAQHAQEPRLTEGAQMNEGVVSAELGLDGWPAVAEESIIARDVLLAEHVGSRVHICHLSTAGSVEIVRWAKSRGIQVTAEVTPHHLLLTDELVRTYNPVYKVNPPLRTERDVMALREALADGTIDIVATDHAPHPHEDKDCEWAAAAMGMVGLETALSVVQETMVDTGLLDWAGVADRMSAKPAQIGQATGHGRPVSAGEPANLTLVDTAYRGQVDPAGFASRSRNTPYQGRELPGRVTHTWLRGKA |
Sequence similarities
Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length755
- Mass (Da)80,901
- Last updated2016-11-02 v1
- ChecksumE897B145E7EFCFC6