E6MV02 · E6MV02_NEIMH

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 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 site709ATP 2 (UniProtKB | ChEBI)
Binding site748ATP 2 (UniProtKB | ChEBI)
Binding site750ATP 2 (UniProtKB | ChEBI)
Binding site755ATP 2 (UniProtKB | ChEBI)
Binding site780ATP 2 (UniProtKB | ChEBI)
Binding site781ATP 2 (UniProtKB | ChEBI)
Binding site782ATP 2 (UniProtKB | ChEBI)
Binding site783ATP 2 (UniProtKB | ChEBI)
Binding site823ATP 2 (UniProtKB | ChEBI)
Binding site823Mg2+ 3 (UniProtKB | ChEBI)
Binding site823Mn2+ 3 (UniProtKB | ChEBI)
Binding site835ATP 2 (UniProtKB | ChEBI)
Binding site835Mg2+ 4 (UniProtKB | ChEBI)
Binding site835Mg2+ 3 (UniProtKB | ChEBI)
Binding site835Mn2+ 4 (UniProtKB | ChEBI)
Binding site835Mn2+ 3 (UniProtKB | ChEBI)
Binding site837Mg2+ 4 (UniProtKB | ChEBI)
Binding site837Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (ammonia) activity
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular FunctionDNA binding
Molecular Functionmetal ion binding
Biological Process'de novo' UMP biosynthetic process
Biological Processarginine biosynthetic process
Biological Processregulation of DNA-templated transcription

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
      NMH_0007

Organism names

Accessions

  • Primary accession
    E6MV02

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.

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-403Carboxyphosphate synthetic domain
Domain133-328ATP-grasp
Domain429-453HTH merR-type
Domain673-864ATP-grasp
Domain931-1071MGS-like
Region931-1071Allosteric 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
    1,071
  • Mass (Da)
    117,376
  • Last updated
    2011-03-08 v1
  • Checksum
    6BBE498935B974EE
MPKRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYKVILVNSNPATIMTDPEMADVTYIEPIMWQTVEKIIAKERPDAILPTMGGQTALNCALDLARNGVLAKYNVELIGATEDAIDKAEDRGRFKEAMEKIGLSCPKSFVCHTMNEALAAQEQVGFPTLIRPSFTMGGSGGGIAYNKDEFLAICERGFDASPTHELLIEQSVLGWKEYEMEVVRDKNDNCIIICSIENFDPMGVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFAVNPANGEMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGFTLDELRNDITGGKTPASFEPSIDYVVTKIPRFAFEKFPAADDRLTTQMKSVGEVMAMGRTIQESFQKALRGLETGLCGFNPRSEDKAEIRRELANPGPERMLFVADAFRAGFTLEEIHEICAIDPWFLAQIEDLMKEEKAVSDGILSDLDFAALRRLKRKGFSDKRLAQLLNVSEKEVREHRYALKLHPVYKRVDTCAAEFATETAYLYSTYEEECESRPSDRKKVMILGGGPNRIGQGIEFDYCCVHAALALRESGFETIMVNCNPETVSTDFDTSDRLYFEPLTLEDVLEIVRTENPWGVIVHYGGQTPLKLANALVENGVNIIGTSADSIDAAEDRERFQKVLNDLGLRQPPNRIAHNEEEALVKAEEIGYPLVVRPSYVLGGRAMQVVHSAEELQKYMREAVQVSEDSPVLLDFFLNNAIEVDVDCVSDGKDVVIGGIMQHVEQAGIHSGDSGCSLPPYSLSEEIQDEIRRQTKAMAYALGVVGLMNVQFAVQDGVVFVLEVNPRASRTVPFVSKATGVPLAKVGARCMAGISLKEQGVEKEVVPDFYAVKEAVFPFIKFPGVDTILGPEMRSTGEVMGVGASFGEAYYKAQLGAGERLNPTGKIFLSVREEDKERVIKTAKNFQVLGYGICATRGTAQYLTEHGLIVQTINKVPEGRPHIGDALKNGEIALVVNTVSSDPQSVSDSHIIRQSALQQRVPQYTTTAGGEAMSEGAKSRDHLGVYSVQELHGRLKNRN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEQZ01000011
EMBL· GenBank· DDBJ
EFV64409.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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