C9RKD9 · C9RKD9_FIBSS

Function

function

Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway.

Catalytic activity

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.

Features

Showing features for binding site.

131320406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site59carbamoyl phosphate (UniProtKB | ChEBI)
Binding site60carbamoyl phosphate (UniProtKB | ChEBI)
Binding site87L-aspartate (UniProtKB | ChEBI)
Binding site109carbamoyl phosphate (UniProtKB | ChEBI)
Binding site137carbamoyl phosphate (UniProtKB | ChEBI)
Binding site140carbamoyl phosphate (UniProtKB | ChEBI)
Binding site170L-aspartate (UniProtKB | ChEBI)
Binding site225L-aspartate (UniProtKB | ChEBI)
Binding site266carbamoyl phosphate (UniProtKB | ChEBI)
Binding site267carbamoyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionamino acid binding
Molecular Functionaspartate carbamoyltransferase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Process'de novo' UMP biosynthetic process
Biological Processamino acid metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartate carbamoyltransferase
  • EC number
  • Alternative names
    • Aspartate transcarbamylase
      (ATCase
      )

Gene names

    • Name
      pyrB
    • Ordered locus names
      FSU_0665

Organism names

Accessions

  • Primary accession
    C9RKD9

Proteomes

Subcellular Location

Interaction

Subunit

Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2).

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-150Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain156-303Aspartate/ornithine carbamoyltransferase Asp/Orn-binding

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    313
  • Mass (Da)
    34,525
  • Last updated
    2009-11-24 v1
  • MD5 Checksum
    CA7DB91119E5212D838D1919D208704B
MSALEIKHLFGLRGVSKHDIRLILDHAKQFREILERPVKKVPSLRGMTVVNLFFENSTRTRTSFELAEKRLSADTVNFASSNSSVKKGETLVDTLRNIEAMKIDIVVVRHKGTGVPKFLADNSNAIIVNAGDGAHEHPTQALLDMLTIEEKLGTLEGKNVTIIGDIRHSRVARSNLWGMSTMGAHVTLCGPSTLVPRNTDLMNHVTWEPDVKKAVANADAIIALRLQKERMDDALLPSMREYRNTFGITEELLECAKDKVIIMHPGPINRGVELDSDIADGEHSVILDQVTNGVAVRMAVLFLLAGGRNNENA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002158
EMBL· GenBank· DDBJ
ADL25889.1
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.
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