A0A1C5ESV9 · A0A1C5ESV9_9ACTN

  • Protein
    Multifunctional fusion protein
  • Gene
    pyrC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

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

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site55carbamoyl phosphate (UniProtKB | ChEBI)
Binding site56carbamoyl phosphate (UniProtKB | ChEBI)
Binding site83L-aspartate (UniProtKB | ChEBI)
Binding site105carbamoyl phosphate (UniProtKB | ChEBI)
Binding site135carbamoyl phosphate (UniProtKB | ChEBI)
Binding site138carbamoyl phosphate (UniProtKB | ChEBI)
Binding site176L-aspartate (UniProtKB | ChEBI)
Binding site230L-aspartate (UniProtKB | ChEBI)
Binding site271carbamoyl phosphate (UniProtKB | ChEBI)
Binding site272carbamoyl phosphate (UniProtKB | ChEBI)
Binding site383Zn2+ 1 (UniProtKB | ChEBI)
Binding site385Zn2+ 1 (UniProtKB | ChEBI)
Binding site385-387substrate
Binding site417substrate
Binding site477Zn2+ 1 (UniProtKB | ChEBI)
Binding site477Zn2+ 2 (UniProtKB | ChEBI)
Binding site504Zn2+ 2 (UniProtKB | ChEBI)
Binding site557Zn2+ 2 (UniProtKB | ChEBI)
Binding site603substrate
Active site630
Binding site630Zn2+ 1 (UniProtKB | ChEBI)
Binding site634substrate

GO annotations

AspectTerm
Molecular Functionamino acid binding
Molecular Functionaspartate carbamoyltransferase activity
Molecular Functiondihydroorotase activity
Molecular Functionzinc ion binding
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
    Multifunctional fusion protein

Including 2 domains:

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

Gene names

    • Name
      pyrC
    • Synonyms
      pyrB
    • ORF names
      GA0115256_138746

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DconLS
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    A0A1C5ESV9

Proteomes

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
Domain3-147Aspartate/ornithine carbamoyltransferase carbamoyl-P binding
Domain163-309Aspartate/ornithine carbamoyltransferase Asp/Orn-binding
Domain374-747Amidohydrolase-related

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    755
  • Mass (Da)
    80,901
  • Last updated
    2016-11-02 v1
  • Checksum
    E897B145E7EFCFC6
MQRHLISAADLSRDDAVLILDTAEEMARVADRPIKKLPTLRGRTVVNLFFEDSTRTRISFEAAEKRLSADVINFSAKGSSVSKGESLKDTAQTLEAMGVDAVVIRHGASGAPYRLATSGWIDAAVINAGDGTHQHPTQALLDAFTMRRRLVGRDAGLGRDLAGKRVTLVGDVLHSRVARSNVDLLHTLGAEVTLVAPPTLIPVGVESWPCEVSYDLDSTLPKCDAVMMLRVQRERMNAAFFPTEREYSRRYGLDGDRMAKLPEHAIVMHPGPMVRGMEITAEVADSDRCTAVEQVANGVSIRMAVLYLLLGGNEPAAAPFALRRSKNMSKILIRGAKVLGGEQQDVLIDGETIAAVGTGLSAEGAEVIEAEGKVLLPGLVDLHTHLREPGREDSETVLTGTRAAASGGYTAVFAMANTFPVADTAGVVEQVWRLGKEHGYCDVQPIGAVTVGLEGRKLAELGAMHESAAGVTVFSDDGKCVDDAVIMRRALEYVKAFGGIVAQHAQEPRLTEGAQMNEGVVSAELGLDGWPAVAEESIIARDVLLAEHVGSRVHICHLSTAGSVEIVRWAKSRGIQVTAEVTPHHLLLTDELVRTYNPVYKVNPPLRTERDVMALREALADGTIDIVATDHAPHPHEDKDCEWAAAAMGMVGLETALSVVQETMVDTGLLDWAGVADRMSAKPAQIGQATGHGRPVSAGEPANLTLVDTAYRGQVDPAGFASRSRNTPYQGRELPGRVTHTWLRGKATLVDGKLT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FMDI01000338
EMBL· GenBank· DDBJ
SCF98304.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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