A0A5C6LVX6 · A0A5C6LVX6_9BACT

  • Protein
    Aspartate carbamoyltransferase
  • Gene
    pyrB
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site58carbamoyl phosphate (UniProtKB | ChEBI)
Binding site59carbamoyl phosphate (UniProtKB | ChEBI)
Binding site86L-aspartate (UniProtKB | ChEBI)
Binding site108carbamoyl phosphate (UniProtKB | ChEBI)
Binding site136carbamoyl phosphate (UniProtKB | ChEBI)
Binding site139carbamoyl phosphate (UniProtKB | ChEBI)
Binding site169L-aspartate (UniProtKB | ChEBI)
Binding site224L-aspartate (UniProtKB | ChEBI)
Binding site265carbamoyl phosphate (UniProtKB | ChEBI)
Binding site266carbamoyl 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
    • ORF names
      FEF09_16170

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • YS-16
  • Taxonomic lineage
    Bacteria > Bacteroidota > Chitinophagia > Chitinophagales > Chitinophagaceae > Chitinophaga

Accessions

  • Primary accession
    A0A5C6LVX6

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).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-149Aspartate/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)
    34,454
  • Last updated
    2019-11-13 v1
  • Checksum
    F77F59EE83ACCC14
MSLSVNHLLGIRGLQRQDIELIFQTADQFKEVLQRPIKKVPSLRDTTIVNLFFENSTRTRISFELAEKRLGADVVNFSASGSSVSKGETLIDTVNNILSMKVDMVVMRHSASGAPHFLSRHIDVPIVNAGDGINEHPTQALLDAFSIRERLGSVAGKKIAICGDIMHSRVALSNIYCLRQLGAEVTVVGPPTLIPKHMEAALGVNVSYDIRETLQWCDVANVLRIQLERQNTPLFSSLREYSLAYGVNRKLLDSLQKEIIVMHPGPINRGVELDSDVADSGHSIILNQVENGVAVRMAVLYLLSGKKPGKVVE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VOHS01000015
EMBL· GenBank· DDBJ
TWV99525.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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