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Class 1 Family 12

Family 12 Overview

2 experimentally studied proteins

38 sequences in Swiss-Prot

3,837 unique sequences in UniRef100

The Glutamyl-tRNA amido-transferase subunit D family, a group of achaeal enzymes that also contain the Class 1 asparaginase domain

Could also have l‑asparaginase activity and high affinity to l‑asparagine

Clan 4: Family 10, Family 11, Family 12, Family 13,

Reference MonomerA

mono1-12.png

Reference Structure

str1-12.png

Family 12 Motifs
(Q5JI77)

motifs1-12

Experimentally Studied Proteins

Fam ? Class - Clan - Family Alt ? Alternative historical name / classification AN ? UniProt accession number Name ? UniProt entry name, only given here for Swiss-Prot entries EC Organism Cell-Loc AAs Structure PDB Km i for Asn [mM] Vmax i for Asn [μmol/min/mg] Kcat i for Asn [s-1]

Swiss-Prot Sequences

Fam ? Class - Clan - Family Alt ? Alternative historical name / classification AN ? UniProt accession number Name ? UniProt entry name, only given here for Swiss-Prot entries EC Organism Cell-Loc AAs Structure PDB Km i for Asn [mM] Vmax i for Asn [μmol/min/mg] Kcat i for Asn [s-1]

UniRef100 SequencesB

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Representative Sequence Alignment

Motifs Image

Additional Information

Clan 4 is an interesting clan of bacterial and archaeal l‑asparaginases. Some sequences display characteristics of both "type I" and "type II" l‑asparaginases and some are structurally unique.

Sequences in Family 12 are called glutamyl-tRNA(Gln) amidotransferase subunit D. These archaeal enzymes catalyse the transamidation from l‑glutamine to l‑glutamyl-tRNA(Gln) to form l‑glutaminyl-tRNA(Gln). The BLAST search results revealed some bacteria carry the gene coding this protein, too. In addition to the l‑asparaginase domain, they contain ~100 amino acid N-terminal residues. Together with glutamyl-tRNA(Gln) amidotransferase subunit E, they form the mature hetero dimer. l‑Asparagine can also be the substrate of this enzyme, acting as the amide donor.