A0A139QJ43 · A0A139QJ43_STRCV

  • 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

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 4 Mg2+ or Mn2+ ions per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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 site119ATP 1 (UniProtKB | ChEBI)
Binding site159ATP 1 (UniProtKB | ChEBI)
Binding site165ATP 1 (UniProtKB | ChEBI)
Binding site166ATP 1 (UniProtKB | ChEBI)
Binding site198ATP 1 (UniProtKB | ChEBI)
Binding site200ATP 1 (UniProtKB | ChEBI)
Binding site205ATP 1 (UniProtKB | ChEBI)
Binding site231ATP 1 (UniProtKB | ChEBI)
Binding site232ATP 1 (UniProtKB | ChEBI)
Binding site233ATP 1 (UniProtKB | ChEBI)
Binding site274ATP 1 (UniProtKB | ChEBI)
Binding site274Mg2+ 1 (UniProtKB | ChEBI)
Binding site274Mn2+ 1 (UniProtKB | ChEBI)
Binding site288ATP 1 (UniProtKB | ChEBI)
Binding site288Mg2+ 1 (UniProtKB | ChEBI)
Binding site288Mg2+ 2 (UniProtKB | ChEBI)
Binding site288Mn2+ 2 (UniProtKB | ChEBI)
Binding site288Mn2+ 1 (UniProtKB | ChEBI)
Binding site290Mg2+ 2 (UniProtKB | ChEBI)
Binding site290Mn2+ 2 (UniProtKB | ChEBI)
Binding site697ATP 2 (UniProtKB | ChEBI)
Binding site736ATP 2 (UniProtKB | ChEBI)
Binding site738ATP 2 (UniProtKB | ChEBI)
Binding site742ATP 2 (UniProtKB | ChEBI)
Binding site767ATP 2 (UniProtKB | ChEBI)
Binding site768ATP 2 (UniProtKB | ChEBI)
Binding site769ATP 2 (UniProtKB | ChEBI)
Binding site770ATP 2 (UniProtKB | ChEBI)
Binding site810ATP 2 (UniProtKB | ChEBI)
Binding site810Mg2+ 3 (UniProtKB | ChEBI)
Binding site810Mn2+ 3 (UniProtKB | ChEBI)
Binding site822ATP 2 (UniProtKB | ChEBI)
Binding site822Mg2+ 3 (UniProtKB | ChEBI)
Binding site822Mg2+ 4 (UniProtKB | ChEBI)
Binding site822Mn2+ 3 (UniProtKB | ChEBI)
Binding site822Mn2+ 4 (UniProtKB | ChEBI)
Binding site824Mg2+ 4 (UniProtKB | ChEBI)
Binding site824Mn2+ 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
      SCODD09_00406

Organism names

  • Taxonomic identifier
  • Strain
    • DD09
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus > Streptococcus anginosus group

Accessions

  • Primary accession
    A0A139QJ43

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
Region1-391Carboxyphosphate synthetic domain
Domain123-317ATP-grasp
Region537-919Carbamoyl phosphate synthetic domain
Domain661-851ATP-grasp
Domain920-1049MGS-like
Region920-1049Allosteric 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
    1,049
  • Mass (Da)
    115,054
  • Last updated
    2016-05-11 v1
  • Checksum
    964C871564F53248
MVIGSGPIIIGQAAEFDYAGTQACLSLKEEGYSVVLVNSNPATIMTDKEIADKVYIEPITIEFVTRILRKERPDAILPTLGGQTGLNMAMELSRTGILDELGVELLGTKLSAIDQAEDRDLFKQLMEDLEQPIPESDIVNSVDEAVAFAAKIGYPVIVRPAFTLGGTGGGMCADEKELREIAENGLKLSPVTQCLIERSIAGFKEIEYEVMRDSADNALVVCNMENFDPVGIHTGDSIVFAPTQTLSDIENQMLRDASLKIIRALKIEGGCNVQLALDPHSFKYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEMINPVTGTTYAMFEPALDYVVAKIPRFPFDKFEHGERRLGTQMKATGEVMAIGRNIEESLLKACRSLEIGVYHNEMAELADVSDDDLVAKIVKAQDDRLFYLSEAIRRGYSIEELSDLTKIDLFFLDKFLHIFEIETKLAAKVGDIAILKEAKQNGFADRKIADIWQMTADAVRKLRLDNKIIPVYKMVDTCAAEFESATPYFYSTYEWENESIKSEKESVIVLGSGPIRIGQGVEFDYATVHSVKAIQNAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTFEDVMNVIELEQPKGVIVQFGGQTAINLAEPLSHAGVTILGTQVADLDRAEDRDLFEQALKDLNIPQPPGQTATNEEEAVASARKIGFPVLVRPSYVLGGRAMEIVENENDLRSYMRTAVKASPDHPVLVDSYLVGSECEVDAISDGKDVLIPGIMEHIERAGVHSGDSMAVYPPQSLSKEVQATIADYTKRLAIGLNCIGMMNIQFVIKDETVYVIEVNPRASRTVPFLSKVTDIPMAQIATKLILGSSLDEFGYKDGLYPESQTVHVKAPVFSFTKLAKVDSLLGPEMKSTGEVMGTDSTLEKALYKAFEASYFHLPAFGNVIFTIADDTKEEALALARRFSNIGYSILATEGTAKFFKENGIQAQLVEKIGTDDHNDIPAFICKGKVQAIINTVGTKRTADEHGQAIRHSAIEHGIPLFTALDTANAMLQVLESRSFMTEAI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LQXU01000019
EMBL· GenBank· DDBJ
KXU02442.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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