A0A255XZB1 · A0A255XZB1_9PROT
- ProteinCarbamoyl phosphate synthase large chain
- GenecarB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1072 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate.
Catalytic activity
- 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H+ + L-glutamate + phosphate
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 4 Mg2+ or Mn2+ ions per subunit.
Pathway
Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 129 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 169 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 175 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 176 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 208 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 210 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 215 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 241 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 242 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 243 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 285 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 285 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 285 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 299 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 299 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 299 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 299 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 299 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 301 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 301 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 715 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 754 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 756 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 761 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 786 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 787 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 788 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 789 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 829 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 829 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 829 | Mn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 841 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 841 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 841 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 841 | Mn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 841 | Mn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 843 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 843 | Mn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (ammonia) activity | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | metal ion binding | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | arginine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCarbamoyl phosphate synthase large chain
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Elstera
Accessions
- Primary accessionA0A255XZB1
Proteomes
Interaction
Subunit
Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-402 | Carboxyphosphate synthetic domain | ||||
Sequence: MPKRTDISSILIIGAGPIVIGQACEFDYSGAQAVKALRAEGYRVILVNSNPATIMTDPELADATYIEPITPEFVARVIEAERPDALLPTMGGQTALNCALALDANGTLEKFGVELIGAKRDAIEKAEDRQLFREAMEKIGLESPKSHLVTSLEEGRAALAQVGLPAIIRPSFTLGGQGGGIAYNVEEFEAIVAGGIKLSPVGSVLVEESVLGWKEYEMEVVRDRADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRDASIAVLREIGVDTGGSNVQFAVNPENGRMVVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELQNDITKVTPASFEPTIDYIVTKIPRFTFEKFPGASPTLTTSMKSVGEVMAIGRTFAESFQKALRGLE | ||||||
Domain | 133-328 | ATP-grasp | ||||
Sequence: REAMEKIGLESPKSHLVTSLEEGRAALAQVGLPAIIRPSFTLGGQGGGIAYNVEEFEAIVAGGIKLSPVGSVLVEESVLGWKEYEMEVVRDRADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRDASIAVLREIGVDTGGSNVQFAVNPENGRMVVIEMNPRVSRSSALASKATGFPIAKVAAKLAV | ||||||
Domain | 679-870 | ATP-grasp | ||||
Sequence: QVLLQQLGLRQPKNGTARSAEEAEKVAEQVGYPVVIRPSYVLGGRAMEIVHDVEGLRRYVSTAVQVSGTTPVLIDSYLRDAIEVDVDAVSDGKDVLVAGIMEHIEEAGIHSGDSACALPPYSLPPAIIDEIRAQTVQLARALKVIGLMNVQFAVKDQTVYILEVNPRASRTVPFVAKATGRPIAKMAARIMA | ||||||
Domain | 936-1072 | MGS-like | ||||
Sequence: SHLPIAGTCFISVKESDKPAMVPLARSLAGLGFRIVATRGTGAYLKDHGIEVQFVNKVTEGRPDVTDLMRSGEIQLVFNTAEGKVAIADSFSLRRAALTAGIAYMTTVAGARAAVRAIEALRGETMGVRPLQDYFAK | ||||||
Region | 936-1072 | Allosteric domain | ||||
Sequence: SHLPIAGTCFISVKESDKPAMVPLARSLAGLGFRIVATRGTGAYLKDHGIEVQFVNKVTEGRPDVTDLMRSGEIQLVFNTAEGKVAIADSFSLRRAALTAGIAYMTTVAGARAAVRAIEALRGETMGVRPLQDYFAK |
Domain
The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A.
Sequence similarities
Belongs to the CarB family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,072
- Mass (Da)114,475
- Last updated2017-12-20 v1
- ChecksumACDB4D4A8F75D394
Keywords
- Technical term