F7QY07 · F7QY07_9LACO

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

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 4 Mg2+ or Mn2+ ions per subunit.
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

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 site118ATP 1 (UniProtKB | ChEBI)
Binding site158ATP 1 (UniProtKB | ChEBI)
Binding site164ATP 1 (UniProtKB | ChEBI)
Binding site165ATP 1 (UniProtKB | ChEBI)
Binding site197ATP 1 (UniProtKB | ChEBI)
Binding site199ATP 1 (UniProtKB | ChEBI)
Binding site204ATP 1 (UniProtKB | ChEBI)
Binding site230ATP 1 (UniProtKB | ChEBI)
Binding site231ATP 1 (UniProtKB | ChEBI)
Binding site232ATP 1 (UniProtKB | ChEBI)
Binding site273ATP 1 (UniProtKB | ChEBI)
Binding site273Mg2+ 1 (UniProtKB | ChEBI)
Binding site273Mn2+ 1 (UniProtKB | ChEBI)
Binding site287ATP 1 (UniProtKB | ChEBI)
Binding site287Mg2+ 1 (UniProtKB | ChEBI)
Binding site287Mg2+ 2 (UniProtKB | ChEBI)
Binding site287Mn2+ 2 (UniProtKB | ChEBI)
Binding site287Mn2+ 1 (UniProtKB | ChEBI)
Binding site289Mg2+ 2 (UniProtKB | ChEBI)
Binding site289Mn2+ 2 (UniProtKB | ChEBI)
Binding site696ATP 2 (UniProtKB | ChEBI)
Binding site735ATP 2 (UniProtKB | ChEBI)
Binding site737ATP 2 (UniProtKB | ChEBI)
Binding site741ATP 2 (UniProtKB | ChEBI)
Binding site766ATP 2 (UniProtKB | ChEBI)
Binding site767ATP 2 (UniProtKB | ChEBI)
Binding site768ATP 2 (UniProtKB | ChEBI)
Binding site769ATP 2 (UniProtKB | ChEBI)
Binding site809ATP 2 (UniProtKB | ChEBI)
Binding site809Mg2+ 3 (UniProtKB | ChEBI)
Binding site809Mn2+ 3 (UniProtKB | ChEBI)
Binding site821ATP 2 (UniProtKB | ChEBI)
Binding site821Mg2+ 3 (UniProtKB | ChEBI)
Binding site821Mg2+ 4 (UniProtKB | ChEBI)
Binding site821Mn2+ 3 (UniProtKB | ChEBI)
Binding site821Mn2+ 4 (UniProtKB | ChEBI)
Binding site823Mg2+ 4 (UniProtKB | ChEBI)
Binding site823Mn2+ 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
      LRU_00292

Organism names

Accessions

  • Primary accession
    F7QY07

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.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-390Carboxyphosphate synthetic domain
Domain122-316ATP-grasp
Region536-918Carbamoyl phosphate synthetic domain
Domain660-850ATP-grasp
Domain919-1050MGS-like
Region919-1050Allosteric 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
    1,050
  • Mass (Da)
    116,033
  • Last updated
    2011-09-21 v1
  • Checksum
    A8B6DAA9D91E366F
MIGSGPIIIGQAAEFDYSGTQACMALREEGYEVVLVNSNPATIMTDTKIADKVYIEPLTTESVSRILRQEYPDALLPTLGGQIGLNLAIALAKTGILDELHIELLGTKLEAIDQAEDREKFKELMQDLNEPIPASKTVNTVEEALEFADEIGYPVIVRPAFTMGGTGGGMCDNKQQLQEICANGLDLSPATQCLIEKSIKGYKEVEYEVMRDSANNAMVVCSMENFDPVGIHTGDSIVLAPTQTLTDREYQMLRDCALKLIRALKIEGGCNVQLALDPNSYEYNVIEVNPRVSRSSALASKATGYPIAKMAAKIAVGLTLDEIINPVTGTTYAEFEPALDYVVAKIPRWPFDKFPRADRRLGTQMKATGEVMAIGRNAEEAIQKAVRSLEIDEKDLISQEARDASDDEVEDKLFHVQDDRIFYIAEAFRRGFTLEEVNELTKINVYFLDIIKHIVELEAELAHNVGDIEILKTAKYYGYSDHTISKLWDMDEDEVRSLRHENKILPVYKMVDTCAAEFESHTPYFYSSYDEENESIKSDKPSVLVIGSGPIRIGQGVEFDYATVHSVKAIQKAGYEAIVMNSNPETVSTDFSISDKLYFEPLTLEDVLNVIELEQPLGVIVQFGGQTAINLAAGLEAHGVKVLGTTVEDLDRAEDRELFDQVINNLGLKQPIGKTATTQEQVMECAHEIGYPVLVRPSYVLGGRAMEIVNNDAELEEYLSHNAKAEIDHPILVDAYLEGYECEVDAICDGKDVLLPGIMEHIEHAGVHSGDSMAVYPPQSFSQDVKDQIVEATKKLAVALKCIGIMNIQFIIHKGEAYVLEVNPRASRTVPFLSKITGIEMTQVATQVILGKSLKELGFESGLYQESKQVHVKAPVFSFSKLADVDSFLGPEMKSTGEVMGSDFNFEKALYKAFAGANMLLPECGRVLFTIEDKDKNVVLPLAERFAKIGYRIFATRGTAEFLRQNGLHATKVSKIGEEDSNDPAIIKLLMNNEVDLVINTMSHDQEMSSDGFVIRQTAIEHNIALLTSLNTADALLRALENRSFATESL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AFOJ01000002
EMBL· GenBank· DDBJ
EGM53156.1
EMBL· GenBank· DDBJ
Genomic DNA

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