A0A2N0UM83 · A0A2N0UM83_9FIRM
- ProteinMultifunctional fusion protein
- GenecarB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1350 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
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
- (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
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.
Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Features
Showing features for binding site, active site, 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: K | ||||||
Binding site | 210 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
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 | 284 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 284 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 284 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 298 | ATP 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 298 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 298 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 298 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 298 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 300 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 300 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 705 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 744 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 746 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 750 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 775 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 776 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 777 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 778 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 818 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 818 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 818 | Mn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 830 | ATP 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 830 | Mg2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 830 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 830 | Mn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 830 | Mn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 832 | Mg2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 832 | Mn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1081 | substrate | ||||
Sequence: N | ||||||
Binding site | 1132 | substrate | ||||
Sequence: N | ||||||
Active site | 1141 | |||||
Sequence: C | ||||||
Active site | 1141 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 1142-1143 | substrate | ||||
Sequence: GN | ||||||
Binding site | 1233 | substrate | ||||
Sequence: N | ||||||
Site | 1235 | Could be important to modulate the pK values of the two catalytic cysteine residues | ||||
Sequence: H | ||||||
Binding site | 1266 | substrate | ||||
Sequence: N | ||||||
Site | 1284 | Could be important to modulate the pK values of the two catalytic cysteine residues | ||||
Sequence: E | ||||||
Binding site | 1284-1285 | substrate | ||||
Sequence: ER | ||||||
Active site | 1293 | Proton acceptor | ||||
Sequence: C | ||||||
Binding site | 1294-1295 | substrate | ||||
Sequence: GT |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (ammonia) activity | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | diaminopimelate epimerase activity | |
Molecular Function | metal ion binding | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | arginine biosynthetic process | |
Biological Process | glutamine metabolic process | |
Biological Process | lysine biosynthetic process via diaminopimelate |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameDiaminopimelate epimerase
- EC number
- Short namesDAP epimerase
- Alternative names
- Recommended nameCarbamoyl phosphate synthase large chain
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Oscillospiraceae > Ruminococcus
Accessions
- Primary accessionA0A2N0UM83
Proteomes
Subcellular Location
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.
Homodimer.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-401 | Carboxyphosphate synthetic domain | ||||
Sequence: MPLKKNIKRVMVIGSGPIVIGQAAEFDYAGTQACRALKEEGLEVILVNSNPATIMTDNAMADKIYIEPLTLETVKRIIKKERPDSLLSTLGGQTGLTLSMQLAKEGFLDKYNVQLLGANPETIDKAEDRQLFKDTMIEIGQPVIPSLVVTDVESAVKFADEIGYPVIIRPAFTLGGTGGGIVDNEEELREITSNGLELSPITQVLVEKCISGWKEIEFEVMRDSDGNVITVCSMENFDPVGVHTGDSIVIAPTVTLADKEYQMLRSAALNIISALKVEGGCNCQFALNPETFEYAVIEVNPRVSRSSALASKATGYPIAKVAAKIAIGYTLNEIKNAVTGTTYACFEPALDYVVVKFPKWPFDKFVYAKRTLGTQMKATGEVMAIAPTFEQAIMKAVRGAE | ||||||
Domain | 133-327 | ATP-grasp | ||||
Sequence: KDTMIEIGQPVIPSLVVTDVESAVKFADEIGYPVIIRPAFTLGGTGGGIVDNEEELREITSNGLELSPITQVLVEKCISGWKEIEFEVMRDSDGNVITVCSMENFDPVGVHTGDSIVIAPTVTLADKEYQMLRSAALNIISALKVEGGCNCQFALNPETFEYAVIEVNPRVSRSSALASKATGYPIAKVAAKIAI | ||||||
Domain | 669-859 | ATP-grasp | ||||
Sequence: DELLEKYHIKRPRGVTVMTTDEALDVADKIGYPVLLRPSYVLGGQNMIIAFNEDDVKEYMAIILAQNIENPILIDKYLQGTELEVDAICDGEDILIPGIMEHIERAGVHSGDSIAVYPAWNLSDRMTQIIIESSKNLAIELRTKGLVNIQYLIYKDELYVIEVNPRSSRTIPYISKVTGVPMVDLATRAML | ||||||
Domain | 928-1068 | MGS-like | ||||
Sequence: YKMKKKGGVFITVRNSDKAEIGEIAKKYYDLGFRIYATEGTADVLKKYGIDAVSVKKIHESKTNNTLTLIESGKIQYVISTSAKGRIPSRDSVKIRRKTVERNIPCLTSLDTANALADCLKSHYSQHSTELIDINHMREEK | ||||||
Region | 928-1350 | Allosteric domain | ||||
Sequence: YKMKKKGGVFITVRNSDKAEIGEIAKKYYDLGFRIYATEGTADVLKKYGIDAVSVKKIHESKTNNTLTLIESGKIQYVISTSAKGRIPSRDSVKIRRKTVERNIPCLTSLDTANALADCLKSHYSQHSTELIDINHMREEKLMLKFTKMQGIGNDYIYCSTFDQEISNPEALAVRLSDRHFGIGGDGIILVCPSKVADAKMKMYNLDGSEGKMCGNGIRCVGKFLYDHGMVDINEKDEITIETLSGIKKLKAYTSGGKVNRLRVDMGKAILDPKEIPVVLDGDKVVDRPVEIAGKNYNITCVSMGNPHCVVFMDDIDNLDIETVGPEFENDKLFPERVNTEFVTVLDDHTIKMRVWERGSGETWACGTGACAVAVAACENGFCKKGEDIKIKLKGGDLIINYTDETVYMTGNAEKVFEGEVEV |
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.
Belongs to the diaminopimelate epimerase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,350
- Mass (Da)149,394
- Last updated2018-04-25 v1
- ChecksumC49ADBD4D75A4AA1