P08308 · OTCC_PSEAE
- ProteinOrnithine carbamoyltransferase, catabolic
- GenearcB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids336 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the catabolism of arginine. Catalyzes the phosphorolysis of citrulline, the reverse reaction of the biosynthetic one, yielding ornithine and carbamoyl phosphate which serve to generate ATP from ADP (PubMed:2118516, PubMed:4962140).
This catabolic OTCase does not carry out the biosynthetic reaction because of a poor affinity and a marked cooperativity for carbamoyl phosphate (PubMed:2118516).
This catabolic OTCase does not carry out the biosynthetic reaction because of a poor affinity and a marked cooperativity for carbamoyl phosphate (PubMed:2118516).
Miscellaneous
Proceeds by an ordered sequential mechanism with CP identified as the initial reactant.
Catalytic activity
- carbamoyl phosphate + L-ornithine = H+ + L-citrulline + phosphate
Activity regulation
Inhibited by 2-aminopentanoic acid (norvaline). Activated by phosphate and nucleoside monophosphates such as AMP, GMP, CMP, UMP. Allosterically inhibited by the polyamines such as spermidine and putrescine.
pH Dependence
Optimum pH is 7.3.
Pathway
Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 57-60 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: STRT | ||||||
Binding site | 84 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 108 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 135-138 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: HPTQ | ||||||
Binding site | 168 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 232 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236-237 | L-ornithine (UniProtKB | ChEBI) | ||||
Sequence: SM | ||||||
Binding site | 274-275 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: CL | ||||||
Binding site | 321 | carbamoyl phosphate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | amino acid binding | |
Molecular Function | ornithine carbamoyltransferase activity | |
Biological Process | arginine biosynthetic process via ornithine | |
Biological Process | arginine catabolic process to ornithine | |
Biological Process | arginine deiminase pathway | |
Biological Process | citrulline biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOrnithine carbamoyltransferase, catabolic
- EC number
- Short namesOTCase
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionP08308
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene are blocked in the arginine deiminase pathway.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 106 | Loss of homotropic cooperativity; gain of anabolic activity. Conformational change which modifies the catalytic site. This mutant is blocked in the active R (relaxed) state. | ||||
Sequence: E → A or G |
PTM/Processing
Features
Showing features for initiator methionine, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000112986 | 2-336 | Ornithine carbamoyltransferase, catabolic | |||
Sequence: AFNMHNRNLLSLMHHSTRELRYLLDLSRDLKRAKYTGTEQQHLKRKNIALIFEKTSTRTRCAFEVAAYDQGANVTYIDPNSSQIGHKESMKDTARVLGRMYDAIEYRGFKQEIVEELAKFAGVPVFNGLTDEYHPTQMLADVLTMREHSDKPLHDISYAYLGDARNNMGNSLLLIGAKLGMDVRIAAPKALWPHDEFVAQCKKFAEESGAKLTLTEDPKEAVKGVDFVHTDVWVSMGEPVEAWGERIKELLPYQVNMEIMKATGNPRAKFMHCLPAFHNSETKVGKQIAEQYPNLANGIEVTEDVFESPYNIAFEQAENRMHTIKAILVSTLADI |
Proteomic databases
Expression
Induction
During limiting aeration and in the presence of arginine.
Interaction
Structure
Sequence
- Sequence statusComplete
- Length336
- Mass (Da)38,109
- Last updated2007-01-23 v3
- Checksum4E780414EADA4724
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X05637 EMBL· GenBank· DDBJ | CAA29124.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG08557.1 EMBL· GenBank· DDBJ | Genomic DNA |