A0A133SKZ5 · A0A133SKZ5_9FIRM

  • 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 site127ATP 1 (UniProtKB | ChEBI)
Binding site167ATP 1 (UniProtKB | ChEBI)
Binding site173ATP 1 (UniProtKB | ChEBI)
Binding site174ATP 1 (UniProtKB | ChEBI)
Binding site206ATP 1 (UniProtKB | ChEBI)
Binding site208ATP 1 (UniProtKB | ChEBI)
Binding site213ATP 1 (UniProtKB | ChEBI)
Binding site239ATP 1 (UniProtKB | ChEBI)
Binding site240ATP 1 (UniProtKB | ChEBI)
Binding site241ATP 1 (UniProtKB | ChEBI)
Binding site282ATP 1 (UniProtKB | ChEBI)
Binding site282Mg2+ 1 (UniProtKB | ChEBI)
Binding site282Mn2+ 1 (UniProtKB | ChEBI)
Binding site296ATP 1 (UniProtKB | ChEBI)
Binding site296Mg2+ 1 (UniProtKB | ChEBI)
Binding site296Mg2+ 2 (UniProtKB | ChEBI)
Binding site296Mn2+ 2 (UniProtKB | ChEBI)
Binding site296Mn2+ 1 (UniProtKB | ChEBI)
Binding site298Mg2+ 2 (UniProtKB | ChEBI)
Binding site298Mn2+ 2 (UniProtKB | ChEBI)
Binding site705ATP 2 (UniProtKB | ChEBI)
Binding site744ATP 2 (UniProtKB | ChEBI)
Binding site750ATP 2 (UniProtKB | ChEBI)
Binding site775ATP 2 (UniProtKB | ChEBI)
Binding site776ATP 2 (UniProtKB | ChEBI)
Binding site777ATP 2 (UniProtKB | ChEBI)
Binding site778ATP 2 (UniProtKB | ChEBI)
Binding site818ATP 2 (UniProtKB | ChEBI)
Binding site818Mg2+ 3 (UniProtKB | ChEBI)
Binding site818Mn2+ 3 (UniProtKB | ChEBI)
Binding site830ATP 2 (UniProtKB | ChEBI)
Binding site830Mg2+ 3 (UniProtKB | ChEBI)
Binding site830Mg2+ 4 (UniProtKB | ChEBI)
Binding site830Mn2+ 3 (UniProtKB | ChEBI)
Binding site830Mn2+ 4 (UniProtKB | ChEBI)
Binding site832Mg2+ 4 (UniProtKB | ChEBI)
Binding site832Mn2+ 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
      HMPREF3201_00130

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MJR9396C
  • Taxonomic lineage
    Bacteria > Bacillota > Negativicutes > Veillonellales > Veillonellaceae > Megasphaera

Accessions

  • Primary accession
    A0A133SKZ5

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.

TypeIDPosition(s)Description
Region1-399Carboxyphosphate synthetic domain
Domain131-325ATP-grasp
Region545-927Carbamoyl phosphate synthetic domain
Domain669-859ATP-grasp
Domain928-1067MGS-like
Region928-1067Allosteric 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
    1,067
  • Mass (Da)
    117,553
  • Last updated
    2016-06-08 v1
  • Checksum
    7198401771B1FD4E
MVEGLKKVLVIGSGPIIIGQAAEFDYAGTQACRALKEEGLEVVLINSNPATIMTDEDIADRVYVEPISLDYVTEVIEKERPDGLLATLGGQVGLNMAVQLANAGVLEKYNVQLLGTRLSAIEEAEDRELFKKAMNDINQPVPESDIFEDVPSAIEFADKIGYPIIVRPAFTLGGTGGGIAHDEDELFMIATRGIKLSPINQILVERSVAGWKEIEYEVMRDKADNCIIVCNMENVDPVGIHTGDSIVVAPSQTLNDLQYQMLRTASLDIIRRLKIEGGCNVQYALDPNSNQYYVIEVNPRVSRSSALASKATGYPIAKVAAKVATGLTLDQITNAVTGKTTACFEPTLDYCVVKFPRWPFEKFALADKSLGTQMKATGEVMSLDRCFEGALLKAVRSLEIGVNYISMKKLESKSLIDIVELLQKQDDERLFVVAQALRLGISEEKIHYITGYDLWFLHKIKNIIDVEFDLQRNNLTIDNVRLAKRYSMPDAVIAEFTKKTEEEVRQFRVDHGIMPTFKMVDTCAAEFEAATPYYYSCYATEDEVKPLGKKSVIVLGSGPIRIGQGIEFDYCSVHSAWALRKAGMNSIIINNNPETVSTDFDTSDSLYFEPLMVEDVMAVVEKEKPVGVICQFGGQTAINLAAPLAKRGVTVLGTSVDGMDRAEDRERFDEVLAKLNIPRPDGRIATSDKEAMKVASELEFPLIVRPSYVLGGRAMEIVYNEKELERYLREAVIASPDHPILIDEYMVGREVEVDAVADGTDVYIPGIMEQVERAGVHSGDSIAVYPPQHLDDDMIAQIVDYTTRISLELQVKGSVNIQFVVSRGKLYIIEVNPRSSRTVPFLSKVTHFPIVEIATRIALGETLKDMGIHSGLMPAKKHVAAKAPVFSFSKIGLAEIALGPEMKSTGEVMGIGHSYSEALYKAVNGAKMKIPAGGTILVTVADRDKAEALHLAEGFKELGYHIIATEGTGSYFNDHGMPVDIVRKIHEGGQNIATMIRNGKIDLVLNTLTYGKHPERDGFNLRRMAVELAVPCLTSLDTAREVLRVFANKGKNDGYHHVAALQDYDME

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LRVC01000002
EMBL· GenBank· DDBJ
KXA70338.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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