SUPERFAMILY 1.73 HMM library and genome assignments server


Aspartate/ornithine carbamoyltransferase superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a/b) [ 51349] (141)
  Mainly parallel beta sheets (beta-alpha-beta units)
Fold:   ATC-like [ 53670] (2)
  consists of two similar domains related by pseudo dyad; duplication
core: 3 layers, a/b/a, parallel beta-sheet of 4 strands, order 2134
Superfamily:   Aspartate/ornithine carbamoyltransferase [ 53671]
Families:   Aspartate/ornithine carbamoyltransferase [ 53672] (3)


Superfamily statistics
Genomes (1,166) UniProt 15.0 PDB chains (SCOP 1.73)
Domains 2,503 2,987 28
Proteins 2,500 2,985 28


Functional annotation
General category Metabolism
Detailed category Amino acids metabolism and transport

Function annotation of SCOP domain superfamilies
InterPro annotation
Cross references IPR006130 SSF53671 Protein matches
Abstract

This family contains two related enzymes:

  1. Aspartate carbamoyltransferase (ATCase) catalyzes the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides [PubMed3015959]. In prokaryotes ATCase consists of two subunits: a catalytic chain (gene pyrB) and a regulatory chain (gene pyrI), while in eukaryotes it is a domain in a multi- functional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals [PubMed8098212]) that also catalyzes other steps of the biosynthesis of pyrimidines.
  2. Ornithine carbamoyltransferase (OTCase) catalyzes the conversion of ornithine and carbamoyl phosphate to citrulline. In mammals this enzyme participates in the urea cycle [PubMed2662961] and is located in the mitochondrial matrix. In prokaryotes and eukaryotic microorganisms it is involved in the biosynthesis of arginine. In some bacterial species it is also involved in the degradation of arginine [PubMed3109911] (the arginine deaminase pathway).
It has been shown [PubMed6379651] that these two enzymes are evolutionary related. The predicted secondary structure of both enzymes are similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies [PubMed6377306], to be implicated in binding the phosphoryl group of carbamoyl phosphate.


InterPro database

PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

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Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 20 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Aspartate/ornithine carbamoyltransferase domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 20 hidden Markov models representing the Aspartate/ornithine carbamoyltransferase superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Internal database links ]