A0A286CC87 · A0A286CC87_9ACTN

  • 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 site129ATP 1 (UniProtKB | ChEBI)
Binding site175ATP 1 (UniProtKB | ChEBI)
Binding site181ATP 1 (UniProtKB | ChEBI)
Binding site182ATP 1 (UniProtKB | ChEBI)
Binding site214ATP 1 (UniProtKB | ChEBI)
Binding site216ATP 1 (UniProtKB | ChEBI)
Binding site221ATP 1 (UniProtKB | ChEBI)
Binding site247ATP 1 (UniProtKB | ChEBI)
Binding site248ATP 1 (UniProtKB | ChEBI)
Binding site249ATP 1 (UniProtKB | ChEBI)
Binding site291ATP 1 (UniProtKB | ChEBI)
Binding site291Mg2+ 1 (UniProtKB | ChEBI)
Binding site291Mn2+ 1 (UniProtKB | ChEBI)
Binding site305ATP 1 (UniProtKB | ChEBI)
Binding site305Mg2+ 2 (UniProtKB | ChEBI)
Binding site305Mg2+ 1 (UniProtKB | ChEBI)
Binding site305Mn2+ 1 (UniProtKB | ChEBI)
Binding site305Mn2+ 2 (UniProtKB | ChEBI)
Binding site307Mg2+ 2 (UniProtKB | ChEBI)
Binding site307Mn2+ 2 (UniProtKB | ChEBI)
Binding site718ATP 2 (UniProtKB | ChEBI)
Binding site757ATP 2 (UniProtKB | ChEBI)
Binding site759ATP 2 (UniProtKB | ChEBI)
Binding site764ATP 2 (UniProtKB | ChEBI)
Binding site789ATP 2 (UniProtKB | ChEBI)
Binding site790ATP 2 (UniProtKB | ChEBI)
Binding site791ATP 2 (UniProtKB | ChEBI)
Binding site792ATP 2 (UniProtKB | ChEBI)
Binding site832ATP 2 (UniProtKB | ChEBI)
Binding site832Mg2+ 3 (UniProtKB | ChEBI)
Binding site832Mn2+ 3 (UniProtKB | ChEBI)
Binding site844ATP 2 (UniProtKB | ChEBI)
Binding site844Mg2+ 3 (UniProtKB | ChEBI)
Binding site844Mg2+ 4 (UniProtKB | ChEBI)
Binding site844Mn2+ 4 (UniProtKB | ChEBI)
Binding site844Mn2+ 3 (UniProtKB | ChEBI)
Binding site846Mg2+ 4 (UniProtKB | ChEBI)
Binding site846Mn2+ 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
      SAMN06272727_1301

Organism names

  • Taxonomic identifier
  • Strain
    • Ag82_G6-1
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A286CC87

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
Region1-408Carboxyphosphate synthetic domain
Domain137-334ATP-grasp
Domain682-873ATP-grasp
Domain955-1100MGS-like
Region955-1102Allosteric 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
    1,102
  • Mass (Da)
    118,280
  • Last updated
    2017-11-22 v1
  • Checksum
    B14A2719A53D0DBA
MPKRTDIQSVLVIGSGPIVIGQAAEFDYSGTQACRVLKAEGLRVVLVNSNPATIMTDPEIADATYVEPITPEFVEKIIAKERPDALLPTLGGQTALNTAISLHGNGVLEKYGVELIGANVEAINKGEDRDLFKEVVEEVRKKIGHGESARSYICHSMDDVLKGVEELGGYPVVVRPSFTMGGAGSGFAHDEEELRRIAGQGLTLSPTTEVLLEESILGWKEYELELMRDKNDNVVVVCSIENFDPMGVHTGDSITVAPAMTLTDREYQVLRDVGIAIIREVGVDTGGCNIQFAVNPEDGRVIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDITQETPASFEPTLDYVVVKAPRFAFEKFPSADSTLTTTMKSVGEAMAIGRNFTEAFQKALRSLEKKGSQFTFVGEPGDKDQLLRDAVRPTDGRINTVMQAIRAGATPEEVFEYTKIDPWFVDQLFLIKEIADELAEAPELTTDLLGEAKRHGFSDQQIGEIRGLREDVVREVRHALGIRPVYKTVDTCAAEFAAKTPYFYSSYDEETEVASREKPAVIILGSGPNRIGQGIEFDYSCVHASFALSDAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVHAEQQAGPVAGVVVQLGGQTPLGLSQALKDNGVPIVGTSPEAIHAAEDRGAFGRVLAEAGLPAPKHGTATTFAEAKTIADEIGYPVLVRPSYVLGGRGMEIVYDETRLEAYIAESTEISPSRPVLVDRFLDDAIEIDVDALYDGEELYLGGVMEHIEEAGIHSGDSACALPPITLGGFDIKRLRASTEGIAKGVGVRGLINIQFALAGDILYVLEANPRASRTVPFTSKATAVPLAKAAARISLGATIAELRAEGLLPANGDGGELPLDAPISVKEAVMPWSRFRDIHGRGVDTVLGPEMRSTGEVMGIDSVFGTAYAKSQAGAYGPLPTKGRAFISVANRDKRSMIFPARELVAHGFELLATSGTAEVLKRNGINATVVRKQSEGTGPNGEKTIVQLIHDGEVDLIVNTPYGTGGRLDGYDIRTAAVARSVPCLTTVQALAAAVQGIDALNRGDVSVRSLQEHAEHLTAARD

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
OCNA01000001
EMBL· GenBank· DDBJ
SOD44022.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp