A0A426VW54 · A0A426VW54_9BACT

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 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 site283ATP 1 (UniProtKB | ChEBI)
Binding site283Mg2+ 1 (UniProtKB | ChEBI)
Binding site283Mn2+ 1 (UniProtKB | ChEBI)
Binding site297ATP 1 (UniProtKB | ChEBI)
Binding site297Mg2+ 1 (UniProtKB | ChEBI)
Binding site297Mg2+ 2 (UniProtKB | ChEBI)
Binding site297Mn2+ 2 (UniProtKB | ChEBI)
Binding site297Mn2+ 1 (UniProtKB | ChEBI)
Binding site299Mg2+ 2 (UniProtKB | ChEBI)
Binding site299Mn2+ 2 (UniProtKB | ChEBI)
Binding site713ATP 2 (UniProtKB | ChEBI)
Binding site752ATP 2 (UniProtKB | ChEBI)
Binding site754ATP 2 (UniProtKB | ChEBI)
Binding site759ATP 2 (UniProtKB | ChEBI)
Binding site784ATP 2 (UniProtKB | ChEBI)
Binding site785ATP 2 (UniProtKB | ChEBI)
Binding site786ATP 2 (UniProtKB | ChEBI)
Binding site787ATP 2 (UniProtKB | ChEBI)
Binding site827ATP 2 (UniProtKB | ChEBI)
Binding site827Mg2+ 3 (UniProtKB | ChEBI)
Binding site827Mn2+ 3 (UniProtKB | ChEBI)
Binding site839ATP 2 (UniProtKB | ChEBI)
Binding site839Mg2+ 3 (UniProtKB | ChEBI)
Binding site839Mg2+ 4 (UniProtKB | ChEBI)
Binding site839Mn2+ 4 (UniProtKB | ChEBI)
Binding site839Mn2+ 3 (UniProtKB | ChEBI)
Binding site841Mg2+ 4 (UniProtKB | ChEBI)
Binding site841Mn2+ 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
      P794_08390

Organism names

Accessions

  • Primary accession
    A0A426VW54

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
Region1-399Carboxyphosphate synthetic domain
Domain131-326ATP-grasp
Domain677-868ATP-grasp
Domain949-1086MGS-like
Region949-1086Allosteric 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
    1,086
  • Mass (Da)
    119,026
  • Last updated
    2019-05-08 v1
  • Checksum
    8BEED4F72E661A76
MPKREDIKTILLIGSGPIVIGQACEFDYSGTQAAKTLKELGYRVVLINSNPATIMTDPEFAHRTYIEPITEKVIAKIIKKENVDAILPTMGGQTALNVAMSMHDKGMLEGVEFLGANPVAIKKGEDRQEFKEAMIKIGMDLPVSQYAYNMDEAMDAAKKIGFPLIIRASYTLAGGGSGVAYNMDEYKEIVKGGLEASPISEILIEESLLGWKEYEMEVIRDRADNCIIVCSIENFDPMGVHTGDSITIAPALTLTDKEYQNMRDASFKILREVGVDTGGSNVQFSINPETGRMIVIEMNPRVSRSSALASKATGYPIAKVATLLAVGFTLDEITNDITGTPASFEPVIDYIVTKLPRFTFEKFPLADSTLTTAMKSVGEVMSMGRTFKESFQKALCSLETGLIGFNPVKCDGEELVREIRRSNENRMLYVFEGLRRGMSVDAIFDLCKIDRWFLYQLEELTQREKEMDIALLSDAARLREVKSEGFSDAMIAEVINNKEGLSLTENDIYNAREKMGVALEYNEVDTCAAEFKALTPYLYSTTNITKLPEPEKIESKEKKVLVIGGGPNRIGQGIEFDYCCVHAAFALEDMGIKSIMYNCNPETVSTDYDTSDILYFEPIDFEHVRNVIELENPDGVIVHFGGQTPLKLAKNLTAIGAKISGTTAKVIDLAEDRELFSNFIEELGLKQPANGTAFAKDEAMAIANRIGYPVLVRPSFVLGGRGMRTVYNDAELREYMDEAVSVSNDAPVLIDKFLDNAIELDVDAICDGNDVYIGSVMQHIEEAGIHSGDSACSLPPVSIPSELQEEVKEQTAKIALGLGVVGLMNIQYAIHKGEIYLIEVNPRASRTVPFVSKATGVPLAKVATRVMVQGDLKEALRYYDTFNVVNFNKKIMEPILKNHVAVKEAVFPFNKLPGSDLILGPEMKSTGEVMGISNNFGMSFAKSQFASKNNIPLEGKLFISLTENDKSQAGEVGKMFTDLGFEIVATSGTHAALQTAGVKSTKVLKISEGRPNIDDMIKNGEIALAINTSDNKASKDDAKTIRQSVLTNHVAYFTTLAAAKATALAIKELKAQQGALEPQALQDYLT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JQIX01000060
EMBL· GenBank· DDBJ
RRS30134.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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