A0A158JYH2 · A0A158JYH2_9BURK

  • Protein
    Carbamoyl phosphate synthase large chain
  • Gene
    carB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Binding site129ATP 1 (UniProtKB | ChEBI)
Binding site176ATP 1 (UniProtKB | ChEBI)
Binding site182ATP 1 (UniProtKB | ChEBI)
Binding site183ATP 1 (UniProtKB | ChEBI)
Binding site215ATP 1 (UniProtKB | ChEBI)
Binding site217ATP 1 (UniProtKB | ChEBI)
Binding site222ATP 1 (UniProtKB | ChEBI)
Binding site248ATP 1 (UniProtKB | ChEBI)
Binding site249ATP 1 (UniProtKB | ChEBI)
Binding site250ATP 1 (UniProtKB | ChEBI)
Binding site292ATP 1 (UniProtKB | ChEBI)
Binding site292Mg2+ 1 (UniProtKB | ChEBI)
Binding site292Mn2+ 1 (UniProtKB | ChEBI)
Binding site306ATP 1 (UniProtKB | ChEBI)
Binding site306Mg2+ 1 (UniProtKB | ChEBI)
Binding site306Mg2+ 2 (UniProtKB | ChEBI)
Binding site306Mn2+ 2 (UniProtKB | ChEBI)
Binding site306Mn2+ 1 (UniProtKB | ChEBI)
Binding site308Mg2+ 2 (UniProtKB | ChEBI)
Binding site308Mn2+ 2 (UniProtKB | ChEBI)
Binding site716ATP 2 (UniProtKB | ChEBI)
Binding site755ATP 2 (UniProtKB | ChEBI)
Binding site757ATP 2 (UniProtKB | ChEBI)
Binding site762ATP 2 (UniProtKB | ChEBI)
Binding site787ATP 2 (UniProtKB | ChEBI)
Binding site788ATP 2 (UniProtKB | ChEBI)
Binding site789ATP 2 (UniProtKB | ChEBI)
Binding site790ATP 2 (UniProtKB | ChEBI)
Binding site830ATP 2 (UniProtKB | ChEBI)
Binding site830Mg2+ 3 (UniProtKB | ChEBI)
Binding site830Mn2+ 3 (UniProtKB | ChEBI)
Binding site851ATP 2 (UniProtKB | ChEBI)
Binding site851Mg2+ 4 (UniProtKB | ChEBI)
Binding site851Mg2+ 3 (UniProtKB | ChEBI)
Binding site851Mn2+ 3 (UniProtKB | ChEBI)
Binding site851Mn2+ 4 (UniProtKB | ChEBI)
Binding site853Mg2+ 4 (UniProtKB | ChEBI)
Binding site853Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (ammonia) activity
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functionmetal ion binding
Biological Process'de novo' UMP biosynthetic process
Biological Processarginine biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Carbamoyl phosphate synthase large chain
  • EC number
  • Alternative names
    • Carbamoyl phosphate synthetase ammonia chain

Gene names

    • Name
      carB
    • ORF names
      AWB74_04560

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • LMG 29317
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Caballeronia

Accessions

  • Primary accession
    A0A158JYH2

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.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-410Carboxyphosphate synthetic domain
Domain133-335ATP-grasp
Domain680-880ATP-grasp
Domain947-1084MGS-like
Region947-1084Allosteric domain

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,084
  • Mass (Da)
    118,746
  • Last updated
    2016-06-08 v1
  • Checksum
    B1E1E994EC4268BF
MPKRTDIKSILIIGAGPIIIGQACEFDYSGAQACKALREEGYKVILVNSNPATIMTDPNTADVTYIEPISWEVVERIIAKERPDAILPTMGGQTALNCALDLFHHGVLEKYKVELIGASPEAIDKAEDRQKFKDAMTKIGLGSAKSGIAHSMEEALAVQAQIAEATGSGGYPTVIRPSFTLGGSGGGIAYNKEEFEEICRRGLDLSPTRELLIEESLLGWKEYEMEVVRDKKDNCIIVCSIENLDPMGVHTGDSITVAPAQTLTDKEYQVLRNASLAVLREIGVDTGGSNVQFAINPNDGRMVVIEMNPRVSRSSALASKATGFPIAKVAAKLACGYTLDELKNEITGGQTPASFEPTIDYVVTKVPRFAFEKFREADSRLTTQMKSVGEVMAMGRTFQESFQKALRGLEVGVDGLDEKTTSRDEVIREIGEPGPDRIWYLGDAFRLGLTMQEIFEETSIDPWFLAQIEQIILKEKALVGRKLASLTRDELLYLKKSGFSDRRLAKLTGSNQADVRKKRHELKVRPVYKRVDTCAAEFATKTAYMYSTYEEECEANPTDKKKIMVLGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFESLTLEDVLEIVDLEKPVGVIVQYGGQTPLKLALDLEANGVSIIGTSPDMIDAAEDRERFQKLLKDLDLRQPPNRTARAEDEALKLAEEIGYPLVVRPSYVLGGRAMEIVHEPRDLERYMREAVKVSNDSPVLLDRFLNDAIECDVDCISDGDDVFIGGVMEHIEQAGVHSGDSACSLPPYSLSKDTVDELKRQTAAMAKALNVVGLMNVQFAIQQVPQPDGSKQDIIYVLEVNPRASRTVPYVSKATSLPLAKIAARAMVGQKLKQQGVTKEVIPPYFSVKEAVFPFVKFPAVDPVLGPEMRSTGEVMGVGRTFGEALFKSQLAAGSRLPESGTVLLTVMDADKPKAVEVAQMLHELGYPIVATKGTAAAIAAAGVPVKVVNKVKDGRPHIVDMIKNGEIALVFTTVDETRAAIADSRSIRMSAQANKVTYYTTMSGARAAVEGLRYLRDLEVYDLQGLHARLN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FCOM02000022
EMBL· GenBank· DDBJ
SAL73942.1
EMBL· GenBank· DDBJ
Genomic DNA

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