O60060 · CARA_SCHPO

Function

function

Small subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, the first step of the arginine biosynthetic pathway (Ref.3). The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia (By similarity).

Miscellaneous

In S.pombe, this enzyme is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control. One is linked to the arginine pathway and is designated CPSase A (arg5-arg4), it is localized to mitochondria and repressed by arginine. A second one, CPSase P, is part of a multifunctional protein (ura1) encoding 3 enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase); it is localized to the cytoplasm and feedback inhibited and repressed by pyrimidines. The carbamoyl phosphate synthesized by each synthase is channeled to its respective pathway, in contrast to Saccharomyces cerevisiae, in which the 2 synthases are localized to the cytoplasm and appear to contribute to the formation of a single cellular pool of carbamoyl phosphate.

Catalytic activity

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site88L-glutamine (UniProtKB | ChEBI)
Binding site272L-glutamine (UniProtKB | ChEBI)
Binding site274L-glutamine (UniProtKB | ChEBI)
Active site301Nucleophile
Binding site302L-glutamine (UniProtKB | ChEBI)
Binding site305L-glutamine (UniProtKB | ChEBI)
Binding site343L-glutamine (UniProtKB | ChEBI)
Binding site345L-glutamine (UniProtKB | ChEBI)
Binding site346L-glutamine (UniProtKB | ChEBI)
Active site385
Active site387

GO annotations

AspectTerm
Cellular Componentcarbamoyl-phosphate synthase complex
Cellular Componentcytoplasm
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular Functioncarbamoyl-phosphate synthase (glutamine-hydrolyzing) activity
Molecular Functionglutaminase activity
Biological Process'de novo' pyrimidine nucleobase biosynthetic process
Biological Processarginine biosynthetic process
Biological Processglutamine metabolic process
Biological Processurea cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Carbamoyl phosphate synthase arginine-specific small chain
  • EC number
  • Short names
    CPS-A
  • Alternative names
    • Arginine-specific carbamoyl phosphate synthetase, glutamine chain

Gene names

    • Name
      arg5
    • Synonyms
      cpa1
    • ORF names
      SPBC56F2.09c

Organism names

Accessions

  • Primary accession
    O60060

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-17Mitochondrion
ChainPRO_000029059918-415Carbamoyl phosphate synthase arginine-specific small chain

Proteomic databases

Interaction

Subunit

Heterodimer composed of 2 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.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain225-412Glutamine amidotransferase type-1

Sequence similarities

Belongs to the CarA family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    415
  • Mass (Da)
    45,662
  • Last updated
    1998-08-01 v1
  • Checksum
    9D3AF94026943980
MLRFLKPFPLRFGKRFYSKVPPVTNHERILPKQPSFPTAPAQNEIATLTIRNGPIFHGTSFGANRNVSGEAVFTTSPVGYVESLTDPSYKQQILIFTQPLIGNYGVPDCKKRDENGLLRHFESPHIQCAGVVVNDYATKYSHWTAVESLGEWCAREGVAAITGVDTRAIVTFLREQGSSLAKISIGEEYDANDDEAFINPEEVNLVSQVSTREPFFVSGGDGMLNIAVIDCGVKENILRSLVSRGASVTVFPFDYPIQNVASNYDGIFLTNGPGDPTHLTKTVNNLRELMNTYNGPIMGICMGHQLLALSTGAKTIKLKYGNRGHNIPALDIASGNCHITSQNHGYAVDASTLPAEWKATWTNLNDQSNEGIAHVSRPISSVQFHPEARGGPMDTFYLFDNYIKEAIKYQKSRTA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CU329671
EMBL· GenBank· DDBJ
CAA18888.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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