A0A1V4UC90 · A0A1V4UC90_9EURY

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 site173ATP 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 site282ATP 1 (UniProtKB | ChEBI)
Binding site282Mg2+ 1 (UniProtKB | ChEBI)
Binding site282Mn2+ 1 (UniProtKB | ChEBI)
Binding site294ATP 1 (UniProtKB | ChEBI)
Binding site294Mg2+ 2 (UniProtKB | ChEBI)
Binding site294Mg2+ 1 (UniProtKB | ChEBI)
Binding site294Mn2+ 1 (UniProtKB | ChEBI)
Binding site294Mn2+ 2 (UniProtKB | ChEBI)
Binding site296Mg2+ 2 (UniProtKB | ChEBI)
Binding site296Mn2+ 2 (UniProtKB | ChEBI)
Binding site697ATP 2 (UniProtKB | ChEBI)
Binding site736ATP 2 (UniProtKB | ChEBI)
Binding site738ATP 2 (UniProtKB | ChEBI)
Binding site743ATP 2 (UniProtKB | ChEBI)
Binding site768ATP 2 (UniProtKB | ChEBI)
Binding site769ATP 2 (UniProtKB | ChEBI)
Binding site770ATP 2 (UniProtKB | ChEBI)
Binding site771ATP 2 (UniProtKB | ChEBI)
Binding site811ATP 2 (UniProtKB | ChEBI)
Binding site811Mg2+ 3 (UniProtKB | ChEBI)
Binding site811Mn2+ 3 (UniProtKB | ChEBI)
Binding site823ATP 2 (UniProtKB | ChEBI)
Binding site823Mg2+ 3 (UniProtKB | ChEBI)
Binding site823Mg2+ 4 (UniProtKB | ChEBI)
Binding site823Mn2+ 4 (UniProtKB | ChEBI)
Binding site823Mn2+ 3 (UniProtKB | ChEBI)
Binding site825Mg2+ 4 (UniProtKB | ChEBI)
Binding site825Mn2+ 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
      pycA_2
    • Synonyms
      carB
    • ORF names
      A4E36_00497

Organism names

Accessions

  • Primary accession
    A0A1V4UC90

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
Region1-397Carboxyphosphate synthetic domain
Domain131-323ATP-grasp
Domain661-852ATP-grasp
Domain918-1055MGS-like
Region920-1055Allosteric 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
    1,055
  • Mass (Da)
    116,251
  • Last updated
    2017-06-07 v1
  • Checksum
    DC135FF4D88559E2
MPKKAHIKKVLLIGSGPIQIGQAAEFDFSGSQACRALREEGVKVVLVNSNPATIQTDPEMADEIYIEPIRAEIIEKIIEKERPDGILSGMGGQTGLNMTAELAERGALKGVEILGTPLEAIYQGEDREKFRALMEHIGEPVPRSMILNRLDQVEEALRTVGLPAIIRPAYTLGGSGGGIAHTREELVRIIEIGLSRSRIHQVLVEESVVGWKEIEFEVMRDAGDTCIIVCGMENVDPMGIHTGESVVVAPILTLRDDEFQMLRTAAIKIIRALDVQGGCNIQFAYQDGEYRVIEVNPRVSRSSALASKATGYPIARVAAKIAIGLRLDEITNSVTGCTPASFEPAIDYIVVKVPRWPFDKFKNADRTLTTAMKSTGEVMAIGRTCEEAFKKALRSIDTDTDTHTNPNEIRMILSRPTDERFTTLFDAVRAGFSVEEIADLTRISPFFLEKIRNIVDLEKKLKNTPTREDIRLAKQYGFTNTEIARESGSPIEQVLDMAGEPTYKIVDTCAAEFPARTPYFYSTWDTECEIPKTDRGKILILGSGPIRIGQGIEFDYCTVHAVKALREENVEVHIVNNNPETVSTDFDTSDRLFFEPMLLEDVVNILKKDTYMGVMVQFGGQNAVNLAVPLNDELKKINLPTRILGTTPDSMDIAEDRDRFSLLLGRLGIPSPPNSSAYSLEEARTRAAAIGYPILVRPSYVLGGRAMEIVHDEIELEGYMKEAVRVSRHHPVLIDSFLQNAIELDVDAVCDGEEVLIGGIMEHIEQAGVHSGDSACVIPTQSLSPSILERVKDYTRKIALGLGVVGLVNIQLAVKDDVVYVLEANPRASRTVPFVSKATGIPLAKIAAKTMIGKKLKEMGYREKAYSHVAVKEVLLPFNKLPGVDTVLGPEMKSTGEVMGIDYDFGRAYYKASISADNTIPVEGNIFISISKEQKDEVVPIAKKLKEIGLNLYGTSGTVDYLTEAGIPAQLVRKVQEGSPNVIDLLRRGEIRMIINTPTDKQSRQDHYQIMRVAVDYGVPYITTIQAARAAAMAIEAIKKERITIEPLSHYLGAM

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MVQC01000042
EMBL· GenBank· DDBJ
OPX70425.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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