A0A0Q8N0T9 · A0A0Q8N0T9_9HYPH

  • 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 site222ATP 1 (UniProtKB | ChEBI)
Binding site228ATP 1 (UniProtKB | ChEBI)
Binding site229ATP 1 (UniProtKB | ChEBI)
Binding site261ATP 1 (UniProtKB | ChEBI)
Binding site263ATP 1 (UniProtKB | ChEBI)
Binding site268ATP 1 (UniProtKB | ChEBI)
Binding site294ATP 1 (UniProtKB | ChEBI)
Binding site295ATP 1 (UniProtKB | ChEBI)
Binding site296ATP 1 (UniProtKB | ChEBI)
Binding site338ATP 1 (UniProtKB | ChEBI)
Binding site338Mg2+ 1 (UniProtKB | ChEBI)
Binding site338Mn2+ 1 (UniProtKB | ChEBI)
Binding site352ATP 1 (UniProtKB | ChEBI)
Binding site352Mg2+ 2 (UniProtKB | ChEBI)
Binding site352Mg2+ 1 (UniProtKB | ChEBI)
Binding site352Mn2+ 1 (UniProtKB | ChEBI)
Binding site352Mn2+ 2 (UniProtKB | ChEBI)
Binding site354Mg2+ 2 (UniProtKB | ChEBI)
Binding site354Mn2+ 2 (UniProtKB | ChEBI)
Binding site779ATP 2 (UniProtKB | ChEBI)
Binding site839ATP 2 (UniProtKB | ChEBI)
Binding site841ATP 2 (UniProtKB | ChEBI)
Binding site846ATP 2 (UniProtKB | ChEBI)
Binding site871ATP 2 (UniProtKB | ChEBI)
Binding site872ATP 2 (UniProtKB | ChEBI)
Binding site873ATP 2 (UniProtKB | ChEBI)
Binding site874ATP 2 (UniProtKB | ChEBI)
Binding site914ATP 2 (UniProtKB | ChEBI)
Binding site914Mg2+ 3 (UniProtKB | ChEBI)
Binding site914Mn2+ 3 (UniProtKB | ChEBI)
Binding site926ATP 2 (UniProtKB | ChEBI)
Binding site926Mg2+ 4 (UniProtKB | ChEBI)
Binding site926Mg2+ 3 (UniProtKB | ChEBI)
Binding site926Mn2+ 4 (UniProtKB | ChEBI)
Binding site926Mn2+ 3 (UniProtKB | ChEBI)
Binding site928Mg2+ 4 (UniProtKB | ChEBI)
Binding site928Mn2+ 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
      ASE04_13315

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Root708
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium

Accessions

  • Primary accession
    A0A0Q8N0T9

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.

Type
IDPosition(s)Description
Region1-456Carboxyphosphate synthetic domain
Domain185-381ATP-grasp
Domain743-955ATP-grasp
Domain1027-1162MGS-like
Region1027-1162Allosteric 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
    1,162
  • Mass (Da)
    125,829
  • Last updated
    2016-01-20 v1
  • Checksum
    7A6A929EBBEB4D00
MPKRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALKEEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAKERPDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPAAIDMAEDRALFREAMQRIGLETPKSMLANATDIKDADRKTHEVERNKLKESLSGAELDTALDALENQWNLGETDRKQRYISHAMAIAAQAIDVVGLPAIIRPSFTMGGTGGGIAYNRSEFFEIIGGGLDASPTTEVLIEESVLGWKEYEMEVVRDKADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQMMRNASIAVLREIGVETGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDELDNDITGGATPASFEPSIDYVVTKIPRFAFEKFPGASPILTTAMKSVGEVMAIGRTFAESLQKALRGLETGLTGLDEIEIPGVEEGESSQNAIRAAIGTPTPDRLRMVAQALRQGMSPEEVHEGCKIDPWFIAQFKAIVDMEARVREHGLPTDAANLRTLKAMGFSDARLATLSGKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYETPFVGELRSEAEVSAAKKVVILGGGPNRIGQGIEFDYCCCHAAFALRDAGYEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEILRAEQEKGEVVGVIVQFGGQTPLKLAEALEKNGIPILGTAPDMIDLAEDRDRFQKLLVKLDLTQPNNGIAYSVEQARLVATEIGFPLVVRPSYVLGGRAMQILHSESQLQTYLLDTVPELVPEDIKQRYPNDKTGQINTLLGKNPLLFDSYLSNAIEVDVDCLSDGNDAFIAGIMEHIEEAGIHSGDSACSLPPRTLSSEMIDELERQAKSMAKALNVVGLMNVQFAIKDGIVYVLEVNPRASRTVPFVAKTIGAPIAKIAARAMAGEKLDALFSAYGEKPDPRNLKHVAVKEAVFPFARFPGVDTLLGPEMRSTGEVIGLDTDFALAFAKSQLGASVELPRDGTVFVSVRDADKPRVLPAIRVLVGEGFKVLATGGTQRFLAENGIEATKINKVLEGRPHIEDAIRNRQVQLVINTTDGNKAISDSKSLRRATLMQKVPYYTTMAGAEAAAQAIKALRAGNLEVRPLQSYFA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMHV01000042
EMBL· GenBank· DDBJ
KRB50894.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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