A0A0M0KPC5 · A0A0M0KPC5_9BACI

  • 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.
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 site129ATP 1 (UniProtKB | ChEBI)
Binding site169ATP 1 (UniProtKB | ChEBI)
Binding site175ATP 1 (UniProtKB | ChEBI)
Binding site176ATP 1 (UniProtKB | ChEBI)
Binding site208ATP 1 (UniProtKB | ChEBI)
Binding site210ATP 1 (UniProtKB | ChEBI)
Binding site215ATP 1 (UniProtKB | ChEBI)
Binding site241ATP 1 (UniProtKB | ChEBI)
Binding site242ATP 1 (UniProtKB | ChEBI)
Binding site243ATP 1 (UniProtKB | ChEBI)
Binding site284ATP 1 (UniProtKB | ChEBI)
Binding site284Mg2+ 1 (UniProtKB | ChEBI)
Binding site284Mn2+ 1 (UniProtKB | ChEBI)
Binding site298ATP 1 (UniProtKB | ChEBI)
Binding site298Mg2+ 1 (UniProtKB | ChEBI)
Binding site298Mg2+ 2 (UniProtKB | ChEBI)
Binding site298Mn2+ 2 (UniProtKB | ChEBI)
Binding site298Mn2+ 1 (UniProtKB | ChEBI)
Binding site300Mg2+ 2 (UniProtKB | ChEBI)
Binding site300Mn2+ 2 (UniProtKB | ChEBI)
Binding site707ATP 2 (UniProtKB | ChEBI)
Binding site746ATP 2 (UniProtKB | ChEBI)
Binding site748ATP 2 (UniProtKB | ChEBI)
Binding site752ATP 2 (UniProtKB | ChEBI)
Binding site777ATP 2 (UniProtKB | ChEBI)
Binding site778ATP 2 (UniProtKB | ChEBI)
Binding site779ATP 2 (UniProtKB | ChEBI)
Binding site780ATP 2 (UniProtKB | ChEBI)
Binding site820ATP 2 (UniProtKB | ChEBI)
Binding site820Mg2+ 3 (UniProtKB | ChEBI)
Binding site820Mn2+ 3 (UniProtKB | ChEBI)
Binding site832ATP 2 (UniProtKB | ChEBI)
Binding site832Mg2+ 4 (UniProtKB | ChEBI)
Binding site832Mg2+ 3 (UniProtKB | ChEBI)
Binding site832Mn2+ 4 (UniProtKB | ChEBI)
Binding site832Mn2+ 3 (UniProtKB | ChEBI)
Binding site834Mg2+ 4 (UniProtKB | ChEBI)
Binding site834Mn2+ 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
      AMD01_20615

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 16467
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Priestia

Accessions

  • Primary accession
    A0A0M0KPC5

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-401Carboxyphosphate synthetic domain
Domain133-327ATP-grasp
Region547-929Carbamoyl phosphate synthetic domain
Domain671-861ATP-grasp
Domain930-1070MGS-like
Region930-1070Allosteric 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
    1,070
  • Mass (Da)
    118,368
  • Last updated
    2015-11-11 v1
  • Checksum
    A9FF8E8BA326A6B9
MPKRVDIETILVIGSGPIIIGQAAEFDYAGTQACLALKEEGYRVILVNSNPATIMTDAEIADKVYIEPLTLEFLTSIIRKERPDALLPTLGGQTGLNMAVELSKSGVLDEMNVEILGTKLSAIEQAEDRELFRSLMNELNEPVPASEIIHTLEEAYSFVDQVDYPVIVRPAYTLGGTGGGICHNEKELIEIVSSGLKNSPVTQCLLEKSIAGFKEVEYEVMRDSNDNAIVVCNMENIDPVGIHTGDSIVVAPSQTLSDREYQLLRNASLKIIRALHIEGGCNVQLALDPDSFQYFIIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLDEMINPVTGKTYACFEPALDYVVSKIPRFPFDKFESAKRNLGTQMKATGEVMAIGRTFEESLLKAVRSLETGLCHLELKDADEIDNVLLEKRIRNAGDERIFYVSEALRRGVTIETIHEWSMIDLFFLYKLQKVVQLEMTLKESKGDLSLLQKAKRAGFSDPKIAELWGMSEQELYELRKENHIVPVYKTVDTCAAEFESSTPYFYGTYEDENESIVTDRKSVIVLGSGPIRIGQGIEFDYATVHSVWAIKQAGYEAIIVNSNPETVSTDFSISDKLYFEPLTIEDVMHIIDLEKPYGVVVQFGGQTAINLAEELGKRGVRILGTSLESLDAAEDRKKFERVLSRLDIPQPLGKTATSVEEAVEIAEEIGYPVLVRPSYVLGGRAMEIVYHKEDLLHYMKNAVKVHADHPVLIDRYLTGKEIEVDAIADGETVYIPGIMEHVERAGVHSGDSIAVYPAQTLSEEIKQKIVDYTIRIAKGLNIVGLLNIQFVLSKNEIYVLEVNPRSSRTVPFLSKITRIPMANLATKAMLGQTLKDAGYEIGIHPEEEGVYVKVPVFSFAKLRRVDITLGPEMKSTGEVMGQDTTYEKALYKGLIASGMSIKTYGSVLMTVADKDKEEALEIAKRFYNIGYQILATEGTASFFAQAGIKAKIVNKIGSEENTLVDVIRTGEAQLVINTLTKGKQPARDGFKIRRESVENGIPCLTSLDTANAILRVLETVGFNTQPMRQAVKTREVTYS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LILC01000032
EMBL· GenBank· DDBJ
KOO40711.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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