PROSITE documentation PDOC00494

Amidases signature

Description

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.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

AMIDASES, PS00571; Amidases 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
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00571
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00571
• Scan Swiss-Prot/TrEMBL entries against PS00571
• view ligand binding statistics
Matching PDB structures: 1MT5 2DF4 2DQN 2F2A ... [ALL]

References

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

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