A0A8F5VPB3 · A0A8F5VPB3_METHU

  • Protein
    Carbamoyl phosphate synthase large chain
  • Gene
    carB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 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 site295ATP 1 (UniProtKB | ChEBI)
Binding site295Mg2+ 1 (UniProtKB | ChEBI)
Binding site295Mg2+ 2 (UniProtKB | ChEBI)
Binding site295Mn2+ 1 (UniProtKB | ChEBI)
Binding site295Mn2+ 2 (UniProtKB | ChEBI)
Binding site297Mg2+ 2 (UniProtKB | ChEBI)
Binding site297Mn2+ 2 (UniProtKB | ChEBI)
Binding site699ATP 2 (UniProtKB | ChEBI)
Binding site738ATP 2 (UniProtKB | ChEBI)
Binding site740ATP 2 (UniProtKB | ChEBI)
Binding site745ATP 2 (UniProtKB | ChEBI)
Binding site770ATP 2 (UniProtKB | ChEBI)
Binding site771ATP 2 (UniProtKB | ChEBI)
Binding site772ATP 2 (UniProtKB | ChEBI)
Binding site773ATP 2 (UniProtKB | ChEBI)
Binding site813ATP 2 (UniProtKB | ChEBI)
Binding site813Mg2+ 3 (UniProtKB | ChEBI)
Binding site813Mn2+ 3 (UniProtKB | ChEBI)
Binding site825ATP 2 (UniProtKB | ChEBI)
Binding site825Mg2+ 3 (UniProtKB | ChEBI)
Binding site825Mg2+ 4 (UniProtKB | ChEBI)
Binding site825Mn2+ 4 (UniProtKB | ChEBI)
Binding site825Mn2+ 3 (UniProtKB | ChEBI)
Binding site827Mg2+ 4 (UniProtKB | ChEBI)
Binding site827Mn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
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
      KSK55_05920

Organism names

  • Taxonomic identifier
  • Strain
    • GP1
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Methanomicrobia > Methanomicrobiales > Methanospirillaceae > Methanospirillum

Accessions

  • Primary accession
    A0A8F5VPB3

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.

Type
IDPosition(s)Description
Region1-398Carboxyphosphate synthetic domain
Domain131-324ATP-grasp
Domain663-854ATP-grasp
Domain920-1056MGS-like
Region922-1056Allosteric 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
    1,056
  • Mass (Da)
    115,246
  • Last updated
    2022-01-19 v1
  • Checksum
    673133854B022746
MPRDPSIKKVLLIGSGPIQIGQAAEFDFSGSQACRALREEGVSVVLVNSNPATIQTDPDMADVTYVEPLQADIIAKIIKKEKPDGILSGMGGQTGLNLTAELAEMGALDGVRILGTPLKAIYEGEDREKFRDLMNRIGEPVPRSVIVSSLDQLEHAASVVGFPAIIRPAYTLGGAGGGIAYNFDELRRIVELGIGKSRIHQVLIEESVAGWKEIEFEVMRDANDTCITICGMENVDPMGIHTGESVVVAPILTLRDDEFHLLRNAALKIIRALDVQGGCNIQFAFKKDAEYRVIEVNPRVSRSSALASKATGYPIARVASKIAIGLRLDEILNTVTGKTPASFEPSIDYVVVKVPRWPFDKFKTADRTLTTAMKSTGEVMAIGRCVEEAFLKSIRSLDTDIDHHSVLSEIKMILQRPTDERFGALFDAFRQGMTLEEIADITKITPFWLEKIQNIVNLEKALSIGADTTLIKKAKQYGFSDGEIAQLSGKDVADISAVTGNPVYKMVDTCAAEFPAMTPYFYSTYGDDVCEISHSDKKKVMILGSGPIRIGQGIEFDYCTVHAITALREEGYEVHVVNNNPETVSTDFDTSDRLFFEPMTLEDVSNILQKDSYYGIMVQFGGQNAVNLAVPLKNEIERLKLQTRILGTTPDAMDMAEDRDRFSVLLDSLGIPTPPNGSAYSEKEAFNTAERIGYPVLVRPSYVLGGRAMEIVHDDAELSTYMREAVKVSKSHPVLIDRFLQNAIELDVDAVCDGTDVIIGGIMEHIETAGVHSGDSACVIPPQSLSPQILADVRDYTRKIALGLGVVGLVNIQFAVQGNTVYVLEANPRASRTVPFVAKSVGIPLAKIAARVMMGGKLADLPYKEQEISHVAVKEVLLPFNKLPGVDTVLGPEMKSTGEVMGIDYDFGRAYYKASIAAHNRLPKSGNVFISVTDDLKDQILKVAKTFVENGLSIYATSGTVEFFAEQGVTANLVRKIAEGSPNVLDMLRAGEISLIINNFADKQSRHDHEQIMRIAVDYGIPYITTVQAAVAAAEAINSVKEENLTIEPLQHYLCS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP077107
EMBL· GenBank· DDBJ
QXO95921.1
EMBL· GenBank· DDBJ
Genomic DNA

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