N6VJK1 · N6VJK1_9HYPH

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

Function

function

Small 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 small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia.

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

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, active site.

TypeIDPosition(s)Description
Binding site60L-glutamine (UniProtKB | ChEBI)
Binding site257L-glutamine (UniProtKB | ChEBI)
Binding site259L-glutamine (UniProtKB | ChEBI)
Active site286Nucleophile
Binding site287L-glutamine (UniProtKB | ChEBI)
Binding site290L-glutamine (UniProtKB | ChEBI)
Binding site328L-glutamine (UniProtKB | ChEBI)
Binding site331L-glutamine (UniProtKB | ChEBI)
Active site370
Active site372

GO annotations

AspectTerm
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functionglutaminase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
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 small chain
  • EC number
  • Alternative names
    • Carbamoyl phosphate synthetase glutamine chain

Gene names

    • Name
      carA
    • ORF names
      BBbe_09120

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 91-4
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Bartonellaceae > Bartonella

Accessions

  • Primary accession
    N6VJK1

Proteomes

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
Region1-200CPSase
Domain16-150Carbamoyl-phosphate synthase small subunit N-terminal

Sequence similarities

Belongs to the CarA family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    399
  • Mass (Da)
    43,676
  • Last updated
    2013-06-26 v1
  • Checksum
    11BAFA0A8AED8598
MTQPTLSPKPWCTSKPTALLILADGTVIEGKGAGATGIVEAEICFNTAMTGYEEILTDPSYTKQIVNFTFPHIGNVGINSEDIEDLIPINHHGAVGAVFKADITHPSNYRANENLNQWLKARQIIAICGVDTRALTVLIREKGAQNAIIAHNLNSNFDLNALKKRMQKWSGITNLDLTKKVTSQQLMEWNEKAWTWNQGYSANSKCNFHIVAIDYGIKRNILRLMATQGARVTIVPAHTNAEEILAMNPDGVFLSNGPGDPSATAAYAVPTIKKLIDCNVPLFGICLGHQLLALSVGAKTIKMHQGHHGANHPVKDLTTGKVEITSMNHSFTVDAASLPKHVEETHISLFDGSNCGIQIIGKPVFSVQHHPEASPGPQDSQYLFQRFHNLIVEYKKQPN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGWA01000007
EMBL· GenBank· DDBJ
ENN91217.1
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