A0A1R4EG81 · A0A1R4EG81_9GAMM

  • 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 site169ATP 1 (UniProtKB | ChEBI)
Binding site175ATP 1 (UniProtKB | ChEBI)
Binding site176ATP 1 (UniProtKB | ChEBI)
Binding site208ATP 1 (UniProtKB | ChEBI)
Binding site210ATP 1 (UniProtKB | ChEBI)
Binding site215ATP 1 (UniProtKB | ChEBI)
Binding site241ATP 1 (UniProtKB | ChEBI)
Binding site242ATP 1 (UniProtKB | ChEBI)
Binding site243ATP 1 (UniProtKB | ChEBI)
Binding site285ATP 1 (UniProtKB | ChEBI)
Binding site285Mg2+ 1 (UniProtKB | ChEBI)
Binding site285Mn2+ 1 (UniProtKB | ChEBI)
Binding site299ATP 1 (UniProtKB | ChEBI)
Binding site299Mg2+ 2 (UniProtKB | ChEBI)
Binding site299Mg2+ 1 (UniProtKB | ChEBI)
Binding site299Mn2+ 2 (UniProtKB | ChEBI)
Binding site299Mn2+ 1 (UniProtKB | ChEBI)
Binding site301Mg2+ 2 (UniProtKB | ChEBI)
Binding site301Mn2+ 2 (UniProtKB | ChEBI)
Binding site722ATP 2 (UniProtKB | ChEBI)
Binding site761ATP 2 (UniProtKB | ChEBI)
Binding site763ATP 2 (UniProtKB | ChEBI)
Binding site768ATP 2 (UniProtKB | ChEBI)
Binding site793ATP 2 (UniProtKB | ChEBI)
Binding site794ATP 2 (UniProtKB | ChEBI)
Binding site795ATP 2 (UniProtKB | ChEBI)
Binding site796ATP 2 (UniProtKB | ChEBI)
Binding site836ATP 2 (UniProtKB | ChEBI)
Binding site836Mg2+ 3 (UniProtKB | ChEBI)
Binding site836Mn2+ 3 (UniProtKB | ChEBI)
Binding site848ATP 2 (UniProtKB | ChEBI)
Binding site848Mg2+ 3 (UniProtKB | ChEBI)
Binding site848Mg2+ 4 (UniProtKB | ChEBI)
Binding site848Mn2+ 4 (UniProtKB | ChEBI)
Binding site848Mn2+ 3 (UniProtKB | ChEBI)
Binding site850Mg2+ 4 (UniProtKB | ChEBI)
Binding site850Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
Biological Processglutamine metabolic 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
      A1019T_01452

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Psychrobacter_pasteurii
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Psychrobacter

Accessions

  • Primary accession
    A0A1R4EG81

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-403Carboxyphosphate synthetic domain
Domain133-328ATP-grasp
Domain686-877ATP-grasp
Region944-1092Allosteric domain
Domain947-1088MGS-like

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
    1,092
  • Mass (Da)
    120,043
  • Last updated
    2017-04-12 v1
  • Checksum
    876A174E3652418D
MPKRTDIKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPVMADATYIEPITWQTVERIIDKERPDAILPTMGGQTALNCALDLDKHGVLTKYNVELIGATKDAIEMAEDRDLFDQAMKRIGLECPRAEIAETMEQAFEIQAKLGFPCIIRPSFTMGGSGGGIAYNRDEFIEICERGFDLSPTHQLLIDESLIGWKEYEMEVVRDKNDNCIIICSIENFDPMGVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVETGGSNVQFGVNPKTGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELQNDITGGQTPASFEPSIDYVVTKIPRFNFEKFPQADNILSTQMKSVGEVMAIGRNFQESMHKALRGLETGADGFDEQIDFAALKAGKISEDKVKSEIKQRLTVPTPERIFYIADAFRLGFSVEDVFGFTNIDPWFLVQIEDIVKTEAQVKQLGFGGLTAKNLRKLKRKGLSDLRLAKLLGVSQKQLRKKRWDLEVFPVYKRVDTCAAEFATSTAYMYSTYDEECEANPTDNKKIMVIGGGPNRIGQGIEFDYCCVHAALAMREDGYETIMVNCNPETVSTDYDTSDRLYFESITLEDVLEIVRIEKPEGVIVQFGGQTPLKLARALEAAGVNIIGTSPDAIDRAEDRERFQHMIHQLNLIQPPNALATSLEDGLVKAKDVGYPLVVRPSYVLGGRAMEIVYNEEELKHYLRTAVQASNEAPVLLDRFLDDAVEVDVDCVSDGNEVVIGGIMQHIEQAGVHSGDSACSLPPYSLSDEICDEMRAQTIAMAKELGVVGLMNVQFAVKDGTVYILEVNPRAARTVPFVSKCIGTSLAQVAARCMAGQSLESQQFTKEIKPAFYAVKESVFPFAKFPGVDPILSPEMKSTGEVMGVGKTFGEAFYKSIIGTNERLPGLPEEGENKTVFISVRDSDKPGIAAVAQQLIDYGFNLVATAGTEQYLTEQGIACKRINKVTEGRPHVVDALKNGEIDLIINTTEGKQAQEDSFSIRRNALQSKVFYVTTLGAAEAVCKSYAIKLPFEVYKLQTLHEQAQVAANKG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FUGD01000087
EMBL· GenBank· DDBJ
SJM37480.1
EMBL· GenBank· DDBJ
Genomic DNA

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