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A0AA92CHJ6 · A0AA92CHJ6_9RHOB

  • 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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site182ATP 1 (UniProtKB | ChEBI)
Binding site188ATP 1 (UniProtKB | ChEBI)
Binding site189ATP 1 (UniProtKB | ChEBI)
Binding site221ATP 1 (UniProtKB | ChEBI)
Binding site223ATP 1 (UniProtKB | ChEBI)
Binding site228ATP 1 (UniProtKB | ChEBI)
Binding site254ATP 1 (UniProtKB | ChEBI)
Binding site255ATP 1 (UniProtKB | ChEBI)
Binding site256ATP 1 (UniProtKB | ChEBI)
Binding site298ATP 1 (UniProtKB | ChEBI)
Binding site298Mg2+ 1 (UniProtKB | ChEBI)
Binding site298Mn2+ 1 (UniProtKB | ChEBI)
Binding site312ATP 1 (UniProtKB | ChEBI)
Binding site312Mg2+ 1 (UniProtKB | ChEBI)
Binding site312Mg2+ 2 (UniProtKB | ChEBI)
Binding site312Mn2+ 2 (UniProtKB | ChEBI)
Binding site312Mn2+ 1 (UniProtKB | ChEBI)
Binding site314Mg2+ 2 (UniProtKB | ChEBI)
Binding site314Mn2+ 2 (UniProtKB | ChEBI)
Binding site744ATP 2 (UniProtKB | ChEBI)
Binding site783ATP 2 (UniProtKB | ChEBI)
Binding site785ATP 2 (UniProtKB | ChEBI)
Binding site790ATP 2 (UniProtKB | ChEBI)
Binding site815ATP 2 (UniProtKB | ChEBI)
Binding site816ATP 2 (UniProtKB | ChEBI)
Binding site817ATP 2 (UniProtKB | ChEBI)
Binding site818ATP 2 (UniProtKB | ChEBI)
Binding site858ATP 2 (UniProtKB | ChEBI)
Binding site858Mg2+ 3 (UniProtKB | ChEBI)
Binding site858Mn2+ 3 (UniProtKB | ChEBI)
Binding site870ATP 2 (UniProtKB | ChEBI)
Binding site870Mg2+ 3 (UniProtKB | ChEBI)
Binding site870Mg2+ 4 (UniProtKB | ChEBI)
Binding site870Mn2+ 3 (UniProtKB | ChEBI)
Binding site870Mn2+ 4 (UniProtKB | ChEBI)
Binding site872Mg2+ 4 (UniProtKB | ChEBI)
Binding site872Mn2+ 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
      DD556_13705

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JL2872
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Phaeobacter

Accessions

  • Primary accession
    A0AA92CHJ6

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.

Type
IDPosition(s)Description
Region1-415Carboxyphosphate synthetic domain
Domain133-341ATP-grasp
Domain708-899ATP-grasp
Domain987-1120MGS-like
Region987-1120Allosteric 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
    1,120
  • Mass (Da)
    121,409
  • Last updated
    2024-03-27 v1
  • MD5 Checksum
    1E25F545185DFCB8B305BF539F354660
MPKRTDIQSIMIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPGLADATYIEPITPEVVAKIIEKERPDALLPTMGGQTGLNTSLALEEMGVLEKYGVEMIGAKREAIEMAEDRKLFREAMDRLGLENPRATIITAPTRDNGSADLEAGVQLALEALDEVGLPAIIRPAFTLGGTGGGVAYNREDYIHYCRSGMDASPVNQILVDESLLGWKEYEMEVVRDKADNAIIVCSIENIDPMGVHTGDSITVAPALTLTDKEYQMMRTASIEVLREIGVETGGSNVQWAVNPDDGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPSIDYVVTKIPKFAFEKFPGSEPYLTTAMKSVGETMAIGRTIHESMQKALASMESGLTGFDEVAIPGMTVGQWDEASGDDKAAVIKAISQQTPDRLRTIAQAMRHGLSDDEIQNVTKFDPWFLSRIREIVDAEREVRKNGLPMREDQLRALKMLGFTDARLGALTGRDEDNVRRARHNLGVTAVFKRIDTCAAEFEAQTPYMYSTYEAPMMGEIECESRPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFALTDVGYETIMINCNPETVSTDYDTSDRLYFEPLTFEHVMEILRAEQENGTLHGVIVQFGGQTPLKLANALQDEGIPILGTTPDAIDLAEDRERFQDLVNKLGLKQPHNGIASTDAQALEIAEEIGFPLVIRPSYVLGGRAMEIVRDMDQLKRYIAEAVVVSGDSPVLLDSYLAGAVELDVDAICDGTDVHVAGIMQHIEEAGVHSGDSACSLPPYSLSKDIIEEIKTQTYALAKALNVVGLMNIQFAIKDGEIFLIEVNPRASRTVPFVAKATDSAIASIAARVMAGEKLSAFPQRAPYEPDAGYDVDVPMADPMTLADPDMPWFSVKEAVLPFARFPGVDTLLGPEMRSTGEVMGWDRSFAGAFLKAQMGAGMVLPSEGRAFISIKDADKGATMLEAARTLIEQGFTLVATGGTKAWLDGHGVACEAVNKVYEGRPHVVDLLKDGHVQLLMNTTEGAQAVEDSKEMRSVALYDKIPYFTTAAGAHAAALAIKAQAEGDVQVKSLQG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QEOS01000006
EMBL· GenBank· DDBJ
PVZ46067.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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