Q51742 · OTCA_PYRFU

Function

function

Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis.

Miscellaneous

It interacts physically with carbamoyl-phosphate synthetase (CKase), forming a channeling cluster for carbamoyl phosphate. This prevents the thermodenaturation of carbamoyl phosphate, an extremely thermolabile and potentially toxic metabolic intermediate (PubMed:9501170).

Catalytic activity

Activity regulation

Inhibited by the bisubstrate delta-N-phosphonoacetyl-L-ornithine (PALO).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.13 mML-ornithine
0.13 mMcarbamoyl phosphate

pH Dependence

Optimum pH is 6.5 (at 55 degrees Celsius).

Temperature Dependence

Extreme thermal stability. It maintains about 50% of its activity after heat treatment for 60 minutes at 100 degrees Celsius.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site57-60carbamoyl phosphate (UniProtKB | ChEBI)
Binding site84carbamoyl phosphate (UniProtKB | ChEBI)
Binding site108carbamoyl phosphate (UniProtKB | ChEBI)
Binding site135-138carbamoyl phosphate (UniProtKB | ChEBI)
Binding site166L-ornithine (UniProtKB | ChEBI)
Binding site230L-ornithine (UniProtKB | ChEBI)
Binding site234-235L-ornithine (UniProtKB | ChEBI)
Binding site270-271carbamoyl phosphate (UniProtKB | ChEBI)
Binding site298carbamoyl phosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Functionamino acid binding
Molecular Functionornithine carbamoyltransferase activity
Biological Processarginine biosynthetic process via ornithine
Biological Processcitrulline biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ornithine carbamoyltransferase, anabolic
  • EC number
  • Short names
    OTCase

Gene names

    • Name
      argF
    • Ordered locus names
      PF0594

Organism names

Accessions

  • Primary accession
    Q51742

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis22Decreased heat stability.
Mutagenesis26Increased dissociation of dodecamers into trimers.
Mutagenesis30Increased dissociation of dodecamers into trimers.
Mutagenesis34Increased dissociation of dodecamers into trimers.
Mutagenesis228Becomes active at low temperatures; when associated with G-278.
Mutagenesis241Becomes active at low temperatures; when associated with G-278.
Mutagenesis278Becomes active at low temperatures; when associated with C-228 or D-241.

PTM/Processing

Features

Showing features for initiator methionine, chain.

Type
IDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001130732-315Ornithine carbamoyltransferase, anabolic

Proteomic databases

Interaction

Subunit

Homododecamer (tetramer of trimers).

Protein-protein interaction databases

Family & Domains

Domain

The monomer folds into two domains of similar size. The N-terminal domain is the carbamoylphosphate-binding domain; ornithine binds to the C-terminal domain.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    315
  • Mass (Da)
    35,181
  • Last updated
    2007-01-23 v6
  • MD5 Checksum
    40DC487326283C98CDA56EE6A1ACEE7B
MVVSLAGRDLLCLQDYTAEEIWTILETAKMFKIWQKIGKPHRLLEGKTLAMIFQKPSTRTRVSFEVAMAHLGGHALYLNAQDLQLRRGETIADTARVLSRYVDAIMARVYDHKDVEDLAKYATVPVINGLSDFSHPCQALADYMTIWEKKGTIKGVKVVYVGDGNNVAHSLMIAGTKLGADVVVATPEGYEPDEKVIKWAEQNAAESGGSFELLHDPVKAVKDADVIYTDVWASMGQEAEAEERRKIFRPFQVNKDLVKHAKPDYMFMHCLPAHRGEEVTDDVIDSPNSVVWDQAENRLHAQKAVLALVMGGIKF

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict206in Ref. 1; CAA73260
Sequence conflict209in Ref. 1; CAA67609

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X99225
EMBL· GenBank· DDBJ
CAA67609.1
EMBL· GenBank· DDBJ
Genomic DNA
Y12727
EMBL· GenBank· DDBJ
CAA73260.1
EMBL· GenBank· DDBJ
Genomic DNA
AE009950
EMBL· GenBank· DDBJ
AAL80718.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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