M0L8C3 · M0L8C3_HALJT

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 site128ATP 1 (UniProtKB | ChEBI)
Binding site183ATP 1 (UniProtKB | ChEBI)
Binding site189ATP 1 (UniProtKB | ChEBI)
Binding site190ATP 1 (UniProtKB | ChEBI)
Binding site222ATP 1 (UniProtKB | ChEBI)
Binding site224ATP 1 (UniProtKB | ChEBI)
Binding site229ATP 1 (UniProtKB | ChEBI)
Binding site255ATP 1 (UniProtKB | ChEBI)
Binding site256ATP 1 (UniProtKB | ChEBI)
Binding site257ATP 1 (UniProtKB | ChEBI)
Binding site298ATP 1 (UniProtKB | ChEBI)
Binding site298Mg2+ 1 (UniProtKB | ChEBI)
Binding site298Mn2+ 1 (UniProtKB | ChEBI)
Binding site315ATP 1 (UniProtKB | ChEBI)
Binding site315Mg2+ 2 (UniProtKB | ChEBI)
Binding site315Mg2+ 1 (UniProtKB | ChEBI)
Binding site315Mn2+ 2 (UniProtKB | ChEBI)
Binding site315Mn2+ 1 (UniProtKB | ChEBI)
Binding site317Mg2+ 2 (UniProtKB | ChEBI)
Binding site317Mn2+ 2 (UniProtKB | ChEBI)
Binding site757ATP 2 (UniProtKB | ChEBI)
Binding site796ATP 2 (UniProtKB | ChEBI)
Binding site798ATP 2 (UniProtKB | ChEBI)
Binding site803ATP 2 (UniProtKB | ChEBI)
Binding site828ATP 2 (UniProtKB | ChEBI)
Binding site829ATP 2 (UniProtKB | ChEBI)
Binding site830ATP 2 (UniProtKB | ChEBI)
Binding site831ATP 2 (UniProtKB | ChEBI)
Binding site872ATP 2 (UniProtKB | ChEBI)
Binding site872Mg2+ 3 (UniProtKB | ChEBI)
Binding site872Mn2+ 3 (UniProtKB | ChEBI)
Binding site884ATP 2 (UniProtKB | ChEBI)
Binding site884Mg2+ 4 (UniProtKB | ChEBI)
Binding site884Mg2+ 3 (UniProtKB | ChEBI)
Binding site884Mn2+ 3 (UniProtKB | ChEBI)
Binding site884Mn2+ 4 (UniProtKB | ChEBI)
Binding site886Mg2+ 4 (UniProtKB | ChEBI)
Binding site886Mn2+ 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
      C444_15198

Organism names

Accessions

  • Primary accession
    M0L8C3

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
Region1-418Carboxyphosphate synthetic domain
Domain132-344ATP-grasp
Domain721-913ATP-grasp
Region981-1083Allosteric 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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,083
  • Mass (Da)
    117,766
  • Last updated
    2013-04-03 v1
  • Checksum
    6AE950BC7B1FA339
MTADEDRTILLIGSGPIKIGQAAEFDYSGAQACRALQEEGARVVLVNSNPATIMTDPEMADKVYLEPINTEAISEIIRKENPDGVIAGLGGQTGLNVTAELAEEGVLDEYDVDVMGTPLDTIYATEDRDLFKQRMEDIGEPVPRSTTITLDEGESVTDLDEESLVDRVEAAVDEVGGLPVIARTTYTLGGSGSGVVDEMDELIERVRKGLRLSRNNEVLITESISGWVELEYEVMRDADDSCIIICNMENIDPMGIHTGESTVVTPSQVIPDEGHQEMRDSALKVIRDLGIQGGCNIQFAWHDDGTPGGEYRVVEVNPRVSRSSALASKATGYPIARVTAKVALGKRLHEIENEITGETTAAFEPAIDYVVTKVPRWPIDKFRDTEFELSTAMKSTGEAMSIGRTFPESLLKALRSSEYNPATDFNEIDDAELETEYLEKPTPDRPYAMFEAFCRGYTVAEVVEITDIKEWYVERFKEVADAADAAREGDYETAAQAGFTDQEITALAGGEFNDTHVSWLPADLDEDGGDEPEVEAATDGSGVQIEDVETDTTDRDFKLVDTCAGEFEATTPYYYSTRDPLSGIDRDELQIDPDLESVVVVGGGPIRIGQGVEFDYCSVHAVRALEELGIDAHVVNNNPETVSTDYDTSDGLFFEPVTAEEVADVIEATDADGVMVQFGGQTSVDIGHPLEQELERRGLDCEIMGTSVDAMDLAEDRDRFNKLMAELGISQAEGGSATSKEEALDLAHDIGYPVLVRPSYVLGGRAMDVVYNDEDLETYIEEAVRVSPDKPILVDEFLADAVELDVDAVADEDDVLIGGVMEHVETAGIHSGDSACMIPPRSQEIKDVMPRIREVVEDIADALDTVGLLNVQLAVRDGEVFVLEANPRSSRTVPFISKTAGVPIAKIAAKVMSGATLSELDVQEQIPEQVSVKEVVLPFDRLPGSDPRLGPEMKSTGEVMGTAGSFGKAYQKAQMAVGKAIPLEGTAIVDLPILGFEEHFDVQDFDDYEDTDAIIDAIQSGEVDLVLSRDRDVLEACVEETVTYFSTHESAEAALEAINSADQPLAVQAIDERPKTQREWGAE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOLY01000039
EMBL· GenBank· DDBJ
EMA28724.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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