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A0A371KC60 · A0A371KC60_9EURY

  • 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 site138ATP 1 (UniProtKB | ChEBI)
Binding site193ATP 1 (UniProtKB | ChEBI)
Binding site199ATP 1 (UniProtKB | ChEBI)
Binding site200ATP 1 (UniProtKB | ChEBI)
Binding site232ATP 1 (UniProtKB | ChEBI)
Binding site234ATP 1 (UniProtKB | ChEBI)
Binding site239ATP 1 (UniProtKB | ChEBI)
Binding site265ATP 1 (UniProtKB | ChEBI)
Binding site266ATP 1 (UniProtKB | ChEBI)
Binding site267ATP 1 (UniProtKB | ChEBI)
Binding site308ATP 1 (UniProtKB | ChEBI)
Binding site308Mg2+ 1 (UniProtKB | ChEBI)
Binding site308Mn2+ 1 (UniProtKB | ChEBI)
Binding site325ATP 1 (UniProtKB | ChEBI)
Binding site325Mg2+ 2 (UniProtKB | ChEBI)
Binding site325Mg2+ 1 (UniProtKB | ChEBI)
Binding site325Mn2+ 2 (UniProtKB | ChEBI)
Binding site325Mn2+ 1 (UniProtKB | ChEBI)
Binding site327Mg2+ 2 (UniProtKB | ChEBI)
Binding site327Mn2+ 2 (UniProtKB | ChEBI)
Binding site741ATP 2 (UniProtKB | ChEBI)
Binding site780ATP 2 (UniProtKB | ChEBI)
Binding site782ATP 2 (UniProtKB | ChEBI)
Binding site787ATP 2 (UniProtKB | ChEBI)
Binding site812ATP 2 (UniProtKB | ChEBI)
Binding site813ATP 2 (UniProtKB | ChEBI)
Binding site814ATP 2 (UniProtKB | ChEBI)
Binding site815ATP 2 (UniProtKB | ChEBI)
Binding site855ATP 2 (UniProtKB | ChEBI)
Binding site855Mg2+ 3 (UniProtKB | ChEBI)
Binding site855Mn2+ 3 (UniProtKB | ChEBI)
Binding site872ATP 2 (UniProtKB | ChEBI)
Binding site872Mg2+ 3 (UniProtKB | ChEBI)
Binding site872Mg2+ 4 (UniProtKB | ChEBI)
Binding site872Mn2+ 4 (UniProtKB | ChEBI)
Binding site872Mn2+ 3 (UniProtKB | ChEBI)
Binding site874Mg2+ 4 (UniProtKB | ChEBI)
Binding site874Mn2+ 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
      DEQ67_08355

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Atlit-48N
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax

Accessions

  • Primary accession
    A0A371KC60

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
Region1-428Carboxyphosphate synthetic domain
Domain142-354ATP-grasp
Domain705-901ATP-grasp
Region969-1082Allosteric 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
    1,082
  • Mass (Da)
    117,184
  • Last updated
    2018-11-07 v1
  • MD5 Checksum
    CC9DEA138D2746E12CF7445EE4D05ABB
MTDEDTSTGPQEGTEDRTILLIGSGPIQIGQAAEFDYSGAQACRALREEGARVVLVNSNPATIMTDPEMADKVYIEPITTEAISEIIERERPDGVIAGLGGQTGLNVTAELAEEGVLEEFDVDIMGTPLDTIYATEDRDLFRQRMEKIGQPVPKSTTISLEEGEAVENITEEALVERVEDSVDAVGGLPVISRTTYTLGGSGSGVVHEMDELVSRVRKGLRLSRNSEVLITESISGWVELEYEVMRDADDSCIIICNMENIDPMGIHTGESTVVTPSQVIPDEGHQEMRDAALQVIRELGIQGGCNIQFAWHDDGTPGGEYRVVEVNPRVSRSSALASKATGYPIARVTAKVALGKRLHEITNEITGETTAAFEPAIDYVVTKVPRWPKDKFTDVDFELSTAMKSTGEAMSIGRTFEESLLKALRSSEYDPAADWDEVSDEELEAEYLEKPTPDRPYAIFEAFERGYTTEDVVELTDIHEWYVERFGRVVEAVEAAAEGDFAAAASAGHTNASIAAATGTSVGEVEQNVPGRTYKQVDTCAGEFAAQTPYYYSARKPEFFRGPFEGDSAGNELRVDRDMESVVVVGGGPIRIGQGVEFDYCSVHAVQALRDMGIDAHVVNNNPETVSTDYDTSDGLFFEPITAEEVADVIEAIDADGVMLQFGGQTSVNIGHPLESELDRRGVDCEILGTTIDAMDLAEDRDRFNRLMDDLGILQPEGGSATSEAEALDLANDLGYPVLVRPSYVLGGRAMEIVHSDADLKEYIEEAVRVSPDKPILIDEFLADGVELDVDAVSDGEDVLIGGVMEHVEAAGVHSGDSACMIPPRSLDDETMARVREVTEDIASALDTVGLMNVQLAVKQNEDGSNDVYVLEANPRSSRTVPFVSKATGVPIAKLAAKVMAGNSLADLDVSEQIPEQVSVKEVVLPFDRLPGSDPRLGPEMKSTGEVMGTATSFGKAYEKAQSAANDPIPADGTVYVDLADPEFPDADSEAGQELLDAFNEYYEVLTPEDVDDFLTMLREGDFDFVVSRDRDTLIDCVEEEVSYFSTYASAKAALEARGAADEDIDVLPVGERPRVVANWGQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QEQI01000002
EMBL· GenBank· DDBJ
RDZ31394.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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