A0AAI8MIP1 · A0AAI8MIP1_9BRAD

  • 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 site134ATP 1 (UniProtKB | ChEBI)
Binding site219ATP 1 (UniProtKB | ChEBI)
Binding site225ATP 1 (UniProtKB | ChEBI)
Binding site226ATP 1 (UniProtKB | ChEBI)
Binding site258ATP 1 (UniProtKB | ChEBI)
Binding site260ATP 1 (UniProtKB | ChEBI)
Binding site265ATP 1 (UniProtKB | ChEBI)
Binding site291ATP 1 (UniProtKB | ChEBI)
Binding site292ATP 1 (UniProtKB | ChEBI)
Binding site293ATP 1 (UniProtKB | ChEBI)
Binding site335ATP 1 (UniProtKB | ChEBI)
Binding site335Mg2+ 1 (UniProtKB | ChEBI)
Binding site335Mn2+ 1 (UniProtKB | ChEBI)
Binding site349ATP 1 (UniProtKB | ChEBI)
Binding site349Mg2+ 2 (UniProtKB | ChEBI)
Binding site349Mg2+ 1 (UniProtKB | ChEBI)
Binding site349Mn2+ 2 (UniProtKB | ChEBI)
Binding site349Mn2+ 1 (UniProtKB | ChEBI)
Binding site351Mg2+ 2 (UniProtKB | ChEBI)
Binding site351Mn2+ 2 (UniProtKB | ChEBI)
Binding site775ATP 2 (UniProtKB | ChEBI)
Binding site835ATP 2 (UniProtKB | ChEBI)
Binding site837ATP 2 (UniProtKB | ChEBI)
Binding site842ATP 2 (UniProtKB | ChEBI)
Binding site867ATP 2 (UniProtKB | ChEBI)
Binding site868ATP 2 (UniProtKB | ChEBI)
Binding site869ATP 2 (UniProtKB | ChEBI)
Binding site870ATP 2 (UniProtKB | ChEBI)
Binding site910ATP 2 (UniProtKB | ChEBI)
Binding site910Mg2+ 3 (UniProtKB | ChEBI)
Binding site910Mn2+ 3 (UniProtKB | ChEBI)
Binding site922ATP 2 (UniProtKB | ChEBI)
Binding site922Mg2+ 3 (UniProtKB | ChEBI)
Binding site922Mg2+ 4 (UniProtKB | ChEBI)
Binding site922Mn2+ 3 (UniProtKB | ChEBI)
Binding site922Mn2+ 4 (UniProtKB | ChEBI)
Binding site924Mg2+ 4 (UniProtKB | ChEBI)
Binding site924Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functionmetal ion binding
Biological Processarginine biosynthetic process
Biological Processglutamine metabolic process
Biological Processpyrimidine nucleotide 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
      S23_59800

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • S23321
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium

Accessions

  • Primary accession
    A0AAI8MIP1

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.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-453Carboxyphosphate synthetic domain
Domain138-378ATP-grasp
Domain739-951ATP-grasp
Domain1017-1154MGS-like
Region1017-1154Allosteric 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,154
  • Mass (Da)
    125,447
  • Last updated
    2024-07-24 v1
  • Checksum
    D0C6DA2C561C9407
MPKRTDITTILIIGAGPIVIGQACEFDYSGTQAVKTLKEEGYRIVLVNSNPATIMTDPELADATYIEPITPEIVAKIIEKERHVIPGGFALLPTMGGQTALNCALSLRRQGTLDKFDVEMIGATADAIDKAEDRQLFREAMTKIGLETPKSRLANASALKKSFRDKHQAEREKLSGAALEEHDRQWTLGEGDRRKRYQEYALGQAMMALSEIGLPAIIRPSFTMGGTGGGIAYNKEEFLDIIERGLDASPTNEVLIEESVLGWKEFEMEVVRDKKDNCIIVCSIENFDPMGVHTGDSITVAPALTLTDKEYQIMRDASLAVLREIGVETGGSNVQFGVNPEDGRMVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDEIANDITGGATPASFEPTIDYVVTKIPRFAFEKFPGASTTLTTSMKSVGEVMAIGRTFQESLQKALRGLETGLTGLDEIEIDGLGQGDDKNAIRAALGTPTPNRLLQVAQAMRLGWSNEEIFNSCKIDPWFLGEMRGIVDMEEKIKKSGLPSNAFGMRTLKAMGFSDARLAVLAQIADADVTAKRHALGVRPAFKRIDTCAAEFASPTAYMYSTYESPFAGTVADESQPSDRKKVIILGGGPNRIGQGIEFDYCCCHACFALADAGYETIMVNCNPETVSTDYDTADRLYFEPLTGEDVLEIIATERTNGTLHGVIVQFGGQTPLKLARALEAADVPILGTSPDAIDLAEDRDRFKRVLDKLRLKQPKNGIAYSVEQARLVATDLGLPLVVRPSYVLGGRAMQIIREENQLSDYLLGTLPELVPADVKARYPNDKTGQINTVLGKNPLLFDRYLSDATEVDVDCLSDGKDTFIVGIMEHIEEAGIHSGDSACSLPPYSLDARMIEELERQTRELALGLDVVGLMNVQYAIKDGDIYVLEVNPRASRTVPFVAKVVGTPVAKIAARIMAGEKLADFKLKKAQLKHVGVKESVFPFARFPGVDTVLGPEMRSTGEVMGIDRNFEVAFAKSQLGGGTRVPRKGTVFVSVRESDKTRIAEAVRELHSLGFKVLATSGTARFLTDQGIPTEKVNKVLEGRPHIVDAITNGDVQLVFNTTEGPQALADSRSLRRAALLHKVPYYTTLSGAVAAAQGIRAYLGGDLEVRTLQSYFSET

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP012279
EMBL· GenBank· DDBJ
BAL79169.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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