On the basis of sequence similarity, a number of transferases have been
proposed [1,2,3,4] to belong to a single family. These proteins are:
Serine O-acetyltransferase (EC 184.108.40.206) (SAT) (gene cysE), an enzyme
involved in cysteine biosynthesis.
Azotobacter chroococcum nitrogen fixation protein nifP. NifP is most
probably a SAT involved in the optimization of nitrogenase activity.
Escherichia coli thiogalactoside acetyltransferase (EC 220.127.116.11) (gene
lacA), an enzyme involved in the biosynthesis of lactose.
UDP-N-acetylglucosamine acyltransferase (EC 18.104.22.168) (gene lpxA), an
enzyme involved in the biosynthesis of lipid A, a phosphorylated glycolipid
that anchors the lipopolysaccharide to the outer membrane of the cell.
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-)
(gene lpxD or firA), which is also involved in the biosynthesis of lipid A.
Chloramphenicol O-acetyltransferase (CAT) (EC 22.214.171.124) from Agrobacterium
tumefaciens, Bacillus sphaericus, Escherichia coli plasmid IncFII NR79,
Pseudomonas aeruginosa, Staphylococcus aureus plasmid pIP630. These CAT are
not evolutionary related to the main family of CAT (see <PDOC00093>).
Rhizobium nodulation protein nodL. NodL is an acetyltransferase involved in
the O-acetylation of Nod factors.
Bacterial tetrahydrodipicolinate N-succinyltransferase (EC 126.96.36.199) (gene
dapD) which catalyzes the fourth step in the biosynthesis of
diaminopimelate and lysine from aspartate semialdehyde.
Bacterial N-acetylglucosamine-1-phosphate uridyltransferase (EC 188.8.131.52)
(gene glmU or gcaD or tms), an enzyme involved in peptidoglycan and
Staphylococcus aureus protein capG which is involved in biosynthesis of
type 1 capsular polysaccharide.
Yeast hypothetical protein YJL218w, which is highly similar to Escherichia
Fission yeast hypothetical protein SpAC18B11.09c.
Methanococcus jannaschii hypothetical protein MJ1064.
These proteins have been shown [3,4] to contain a repeat structure composed of
tandem repeats of a [LIV]-G-x(4) hexapeptide which, in the tertiary structure
of lpxA , has been shown to form a left-handed parallel β helix. Our
signature pattern is based on a fourfold repeat of this hexapeptide.
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