A0A2I0TII8 · A0A2I0TII8_LIMLA
- ProteinCad protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2006 (go to sequence)
- Protein existenceInferred from homology
- 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.
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Charadriiformes > Scolopacidae > Limosa
Accessions
- Primary accessionA0A2I0TII8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 309-501 | ATP-grasp | ||||
Sequence: VEKMEEIGEHVAPSEAAASLEQALAAAERLGYPVLVRSAYALGGLGSGFANNREELVALVSQAFTHTSQVLVDKSLKGWKEIEYEVVRDAYNNCITVCNMENLDPLGIHTGESIVVAPSQTLNDTEYFLLRRTAVKVVRHLGIVGECNIQFALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLAL | ||||||
Domain | 845-1036 | ATP-grasp | ||||
Sequence: SRLLDSIGISQPLWKELSDMESAKHFCCKVGYPCVVRPSYVLSGAAMNVAYSDSDLEKFLSNAVAVSKEQPVVISKFIQEAKEIDVDAVACDGVVVAIAISEHVENAGVHSGDATLVTPPQDITPKTLERIKAIVHAVGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALASQVIM | ||||||
Domain | 1101-1259 | MGS-like | ||||
Sequence: FKIPKKNILLTIGSYKNKSELLPTVRTLESLGYKLYASLGTADFYTEHGIKVMAVDWHFEEAEGSEAGARETQQRSILDYLAENHFEMVINLSMRNSGGRRLSSFVTKGYRTRRLAVDYSVPLIIDIKCTKLFVEALGQIGAAPPLKIHVDCMTSQKLI | ||||||
Region | 1641-1677 | Disordered | ||||
Sequence: LRGRASSPRRAGPMGEGRFHLPPRIHRASDPGLPAED | ||||||
Compositional bias | 1660-1677 | Basic and acidic residues | ||||
Sequence: HLPPRIHRASDPGLPAED |
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
- Length2,006
- Mass (Da)220,608
- Last updated2018-02-28 v1
- Checksum362FC0336D0CC09E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1660-1677 | Basic and acidic residues | ||||
Sequence: HLPPRIHRASDPGLPAED |
Keywords
- Technical term