Q0IAV9 · Q0IAV9_SYNS3

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 site170ATP 1 (UniProtKB | ChEBI)
Binding site176ATP 1 (UniProtKB | ChEBI)
Binding site177ATP 1 (UniProtKB | ChEBI)
Binding site209ATP 1 (UniProtKB | ChEBI)
Binding site211ATP 1 (UniProtKB | ChEBI)
Binding site216ATP 1 (UniProtKB | ChEBI)
Binding site242ATP 1 (UniProtKB | ChEBI)
Binding site243ATP 1 (UniProtKB | ChEBI)
Binding site244ATP 1 (UniProtKB | ChEBI)
Binding site286ATP 1 (UniProtKB | ChEBI)
Binding site286Mg2+ 1 (UniProtKB | ChEBI)
Binding site286Mn2+ 1 (UniProtKB | ChEBI)
Binding site300ATP 1 (UniProtKB | ChEBI)
Binding site300Mg2+ 2 (UniProtKB | ChEBI)
Binding site300Mg2+ 1 (UniProtKB | ChEBI)
Binding site300Mn2+ 1 (UniProtKB | ChEBI)
Binding site300Mn2+ 2 (UniProtKB | ChEBI)
Binding site302Mg2+ 2 (UniProtKB | ChEBI)
Binding site302Mn2+ 2 (UniProtKB | ChEBI)
Binding site739ATP 2 (UniProtKB | ChEBI)
Binding site778ATP 2 (UniProtKB | ChEBI)
Binding site780ATP 2 (UniProtKB | ChEBI)
Binding site785ATP 2 (UniProtKB | ChEBI)
Binding site811ATP 2 (UniProtKB | ChEBI)
Binding site812ATP 2 (UniProtKB | ChEBI)
Binding site813ATP 2 (UniProtKB | ChEBI)
Binding site814ATP 2 (UniProtKB | ChEBI)
Binding site854ATP 2 (UniProtKB | ChEBI)
Binding site854Mg2+ 3 (UniProtKB | ChEBI)
Binding site854Mn2+ 3 (UniProtKB | ChEBI)
Binding site871ATP 2 (UniProtKB | ChEBI)
Binding site871Mg2+ 3 (UniProtKB | ChEBI)
Binding site871Mg2+ 4 (UniProtKB | ChEBI)
Binding site871Mn2+ 4 (UniProtKB | ChEBI)
Binding site871Mn2+ 3 (UniProtKB | ChEBI)
Binding site873Mg2+ 4 (UniProtKB | ChEBI)
Binding site873Mn2+ 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
    • Ordered locus names
      sync_1204

Organism names

Accessions

  • Primary accession
    Q0IAV9

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
Region1-403Carboxyphosphate synthetic domain
Domain133-329ATP-grasp
Region406-425Disordered
Domain703-900ATP-grasp
Domain967-1107MGS-like
Region967-1107Allosteric 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
    1,107
  • Mass (Da)
    120,041
  • Last updated
    2006-10-03 v1
  • Checksum
    2EB0F7A3F1CAC0E7
MPRRNDLRRILLLGSGPIVIGQACEFDYSGTQACKALRAEGYEVILINSNPASIMTDPEMADRTYVEPLTPDVVTRVIELERPDALLPTMGGQTALNLAVALSKDGTLDRFGVELIGADLKAIQKAEDRQLFKQAMERIGVHVCPSGIASTLEEAESVGASISSYPRIIRPAFTLGGSGGGIAYNPEEFSAICKTGLDASPVSQILIEKSLLGWKEFELEVMRDLADNVVIVCSIENLDPMGVHTGDSITVAPAQTLTDREYQRLRDQSIAIIREIGVATGGSNIQFAINPADGEVVVIEMNPRVSRSSALASKATGFPIAKIAARLAIGYTLDEILNDITGKTPACFEPTIDYVVTKVPRFAFEKFRGSPAVLTTAMKSVGEAMAIGRCFEESFQKALRSLETGLSGWGGDRPEPSCSKTDLERSLRTPSPDRILAVRSAMLSGMTDAHIHELSHIDPWFLAKLRGLIDAESDLLKGKSLEDLDETILFKLKTLGYSDRQIAWFVDSKELNVRERRDQLGVTPVFKTVDTCAAEFASSTPYHYSTYERPLFRLKPDGLLQPMAPSTEVATETRPKLMILGGGPNRIGQGIEFDYCCCHASFSAQDQGFATVMLNSNPETVSTDYDSSDRLYFEPITLEDVLNVIEAERPNGVIVQFGGQTPLKLALSLLNWLSTPQGKATGTQIWGTSPASIDLAEDREQFEAILRKLEIRQPRNGLARSEVEARSIAGNVGYPVVVRPSYVLGGRAMEVVYDEEELNRYMKEAVQVEPDHPVLIDQYLENAVEVDVDALCDHEGTVVIGGLMEHIEPAGIHSGDSACCLPSISLSEDALSLIRRWSEALAITLKVQGLINLQFAVQRAADGQEKVFIIEANPRASRTVPFVAKATGVPLARLATRLMAGETLSQVGLLKEPVPPLQTVKEAVLPFRRFPGSDSLLGPEMRSTGEVMGSASDFGMAFAKAELAAGEALPTTGTVFLSTHDRDKPALVPVARQLIGLGFQLMATSGTAQALRNEGLQVESVLKVHEGRPNIEDLIRSGGVQLVINTPIGRQAAHDDRYLRRAALDYSVPTLTTLAGARAAVEAIEALQTRTIVIHALQDVHASLSGQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000435
EMBL· GenBank· DDBJ
ABI45798.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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