{PDOC00494}
{PS00571; AMIDASES}
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* Amidases signature *
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It has been shown [1,2,3] that  several  enzymes  from various prokaryotic and
eukaryotic organisms which are involved in the hydrolysis of amides (amidases)
are evolutionary related. These enzymes are listed below.

 - Indoleacetamide hydrolase (EC 3.5.1.-), a  bacterial plasmid-encoded enzyme
   that catalyzes the  hydrolysis  of  indole-3-acetamide (IAM) into indole-3-
   acetate (IAA), the  second  step  in  the   biosynthesis  of   auxins  from
   tryptophan.
 - Acetamidase  from  Emericella nidulans (gene amdS), an  enzyme which allows
   acetamide to be used as a sole carbon or nitrogen source.
 - Amidase (EC 3.5.1.4) from Rhodococcus sp. N-774 and Brevibacterium sp. R312
   (gene amdA). This enzyme hydrolyzes propionamides efficiently,  and also at
   a lower efficiency, acetamide, acrylamide and indoleacetamide.
 - Amidase (EC 3.5.1.4) from Pseudomonas chlororaphis.
 - 6-aminohexanoate-cyclic-dimer  hydrolase  (EC 3.5.2.12)   (nylon  oligomers
   degrading enzyme E1) (gene nylA), a bacterial plasmid  encoded enzyme which
   catalyzes the first  step in the degradation of 6-aminohexanoic acid cyclic
   dimer, a by-product of nylon manufacture [4].
 - Glutamyl-tRNA(Gln) amidotransferase subunit A [5].
 - Mammalian fatty acid amide hydrolase (gene FAAH) [6].
 - A putative amidase from yeast (gene AMD2).
 - Mycobacterium tuberculosis putative amidases amiA2, amiB2, amiC and amiD.

All these enzymes contains in their central  section a highly conserved region
rich in glycine, serine, and alanine residues.  We  have used this region as a
signature pattern.

-Consensus pattern: G-[GAV]-S-[GS](2)-G-x-[GSAE]-[GSAVYCT]-x-[LIVMT]-[GSA]-
                    x(6)-[GSAT]-x-[GA]-x-[DE]-x-[GA]-x-S-[LIVM]-R-x-P-[GSACTL]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2006 / Pattern revised.

[ 1] Mayaux J.-F., Cerebelaud E., Soubrier F., Faucher D., Petre D.
     "Purification, cloning, and primary structure of an
     enantiomer-selective amidase from Brevibacterium sp. strain R312:
     structural evidence for genetic coupling with nitrile hydratase."
     J. Bacteriol. 172:6764-6773(1990).
     PubMed=2254253
[ 2] Hashimoto Y., Nishiyama M., Ikehata O., Horinouchi S., Beppu T.
     "Cloning and characterization of an amidase gene from Rhodococcus
     species N-774 and its expression in Escherichia coli."
     Biochim. Biophys. Acta 1088:225-233(1991).
     PubMed=2001397
[ 3] Chang T.-H., Abelson J.
     "Identification of a putative amidase gene in yeast Saccharomyces
     cerevisiae."
     Nucleic Acids Res. 18:7180-7180(1990).
     PubMed=2263500
[ 4] Tsuchiya K., Fukuyama S., Kanzaki N., Kanagawa K., Negoro S., Okada H.
     "High homology between 6-aminohexanoate-cyclic-dimer hydrolases of
     Flavobacterium and Pseudomonas strains."
     J. Bacteriol. 171:3187-3191(1989).
     PubMed=2722746
[ 5] Curnow A.W., Hong K., Yuan R., Kim S., Martins O., Winkler W.,
     Henkin T.M., Soll D.
     "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required
     for correct decoding of glutamine codons during translation."
     Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997).
     PubMed=9342321
[ 6] Cravatt B.F., Giang D.K., Mayfield S.P., Boger D.L., Lerner R.A.,
     Gilula N.B.
     "Molecular characterization of an enzyme that degrades neuromodulatory
     fatty-acid amides."
     Nature 384:83-87(1996).
     PubMed=8900284

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