A0A023F583 · A0A023F583_TRIIF
- ProteinPutative multifunctional pyrimidine synthesis protein cad includes carbamoyl-phosphate synthetase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids2202 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
Catalytic activity
- (S)-dihydroorotate + H2O = H+ + N-carbamoyl-L-aspartate
Cofactor
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.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 252 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 336 | |||||
Sequence: H | ||||||
Active site | 338 | |||||
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
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Reduviidae > Triatominae > Triatoma
Accessions
- Primary accessionA0A023F583
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 517-709 | ATP-grasp | ||||
Sequence: ADRINEIEEKVAPSAAVYSVNEALDAAMRLGYPVLARSAFSLGGLGSGFANNDDELRKLAQHAFAHSNQLIIDKSLKGWKEVEYEVVRDAFDNCITVCNMENVDPLGIHTGESIVVAPSQTLSNAEYNRLRTTAIKVIRHFGIVGECNIQYALSPTSGEFYIIEVNARLSRSSALASKATGFPLAYVAAKLAL | ||||||
Domain | 1049-1240 | ATP-grasp | ||||
Sequence: SRMLDRIGILQPRWKELTNLKSAMDFCEEVGYPCLVRPSYVLSGAAMSVVHSERDLEEYLALASDVSKEHPVVISKFLQEAKEIDVDAVACDGVILCMAVSEHVENAGVHSGDATLVTPPQDINAETLAKILAISRAVASSLEVTGPFNMQLIAKDNVLKVIECNVRVSRSFPFVSKTLDHDFVATATRVIV | ||||||
Domain | 1305-1461 | MGS-like | ||||
Sequence: FHIPQKAILLSIGSFKHKKELLPSMKSLQKMGYKLYASMGTADFYNEHGVRVEPVQWTFENIGEATTTSGELNNLADFLARKDFDLVINLPMRNRGARRVSSFMTYGYRTRRLAVDFSVPLVTDVKCAKLLVEAMLGTKECPVMKTHTDCLTSRRII |
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 statusFragment
- Length2,202
- Mass (Da)244,558
- Last updated2014-06-11 v1
- ChecksumD5AB3D294A663C9B
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: C |