{PDOC00613} {PS00758; ARGE_DAPE_CPG2_1} {PS00759; ARGE_DAPE_CPG2_2} {BEGIN} ****************************************************** * ArgE / dapE / ACY1 / CPG2 / yscS family signatures * ****************************************************** The following enzymes have been shown [1,2,3] to be evolutionary and functionally related: - In the biosynthetic pathway from glutamate to arginine, the removal of an acetyl group from N2-acetylornithine can be catalyzed via two distinct enzymatic strategies depending on the organism. In some bacteria and in fungi, the acetyl group is transferred on glutamate by glutamate N-acetyltransferase (EC 2.3.1.35) while in enterobacteria such as Escherichia coli, it is hydrolyzed by acetylornithine deacetylase (EC 3.5.1.16) (acetylornithinase) (AO) (gene argE). AO is a homodimeric cobalt-dependent enzyme which displays broad specificity and can also deacylates substrates such as acetylarginine, acetylhistidine, acetylglutamate semialdehyde, etc. - Succinyldiaminopimelate desuccinylase (EC 3.5.1.18) (SDAP) (gene dapE) is the enzyme which catalyzes the fifth step in the biosynthesis of lysine from aspartate semialdehyde: the hydrolysis of succinyl-diaminopimelate to diaminopimelate and succinate. SDAP is an enzyme that requires cobalt or zinc as a cofactor. - Aminoacylase-1 [4] (EC 3.5.1.14) (N-acyl-l-amino-acid amidohydrolase) (ACY1). ACY1 is a homodimeric zinc-binding mammalian enzyme that catalyzes the hydrolysis of N-alpha-acylated amino acids (except for aspartate). - Carboxypeptidase G2 (EC 3.4.17.11) (folate hydrolase G2) (gene cpg2) from Pseudomonas strain RS-16. This enzyme catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and glutamate. G2 is a homodimeric zinc-dependent enzyme. - Vacuolar carboxypeptidase S (EC 3.4.17.4) (yscS) from yeast (gene CPS1). - Peptidase T (EC 3.4.11.-) (gene pepT) (tripeptidase) from bacteria. This enzyme catalyzes a variety of tripeptides containing N-terminal methionine, leucine, or phenylalanine. - Xaa-His dipeptidase (EC 3.4.13.3) (carnosinase) from Lactobacillus (gene pepV) [5], a metalloenzyme with activity against beta-alanyl-dipeptides including carnosine (beta-alanyl-histidine). These enzymes share a few characteristics. They hydrolyse peptidic bonds in substrates that share a common structure, they are dependent on cobalt or zinc for their activity and they are proteins of 40 Kd to 60 Kd with a number of regions of sequence similarity. As signature patterns for these proteins, we selected two of the conserved regions. The first pattern contains a conserved histidine which could be involved in binding metal ions and the second pattern contains a number of conserved charged residues. -Consensus pattern: [LIV]-[GALMY]-[LIVMF]-{Q}-[GSA]-H-x-D-[TV]-[STAV] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: 9. -Consensus pattern: [GSTAI]-[SANQCVIT]-D-x-K-[GSACN]-x(1,2)-[LIVMA]-x(2)- [LIVMFY]-x(12,17)-[LIVM]-x-[LIVMF]-[LIVMSTAGC]-[LIVMFA]- x(2)-[DNGM]-E-E-x(0,1)-[GSTNE] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: These proteins belong to families M20A/M20B in the classification of peptidases [6,E1]. -Last update: December 2004 / Patterns and text revised. [ 1] Meinnel T., Schmitt E., Mechulam Y., Blanquet S. "Structural and biochemical characterization of the Escherichia coli argE gene product." J. Bacteriol. 174:2323-2331(1992). PubMed=1551850 [ 2] Boyen A., Charlier D., Charlier J., Sakanyan V., Mett I., Glansdorff N. "Acetylornithine deacetylase, succinyldiaminopimelate desuccinylase and carboxypeptidase G2 are evolutionarily related." Gene 116:1-6(1992). PubMed=1628835 [ 3] Miller C.G., Miller J.L., Bagga D.A. "Cloning and nucleotide sequence of the anaerobically regulated pepT gene of Salmonella typhimurium." J. Bacteriol. 173:3554-3558(1991). PubMed=1904438 [ 4] Mitta M., Ohnogi H., Yamamoto A., Kato I., Sakiyama F., Tsunasawa S. "The primary structure of porcine aminoacylase 1 deduced from cDNA sequence." J. Biochem. 112:737-742(1992). PubMed=1284246 [ 5] Vongerichten K.F., Klein J.R., Matern H., Plapp R. "Cloning and nucleotide sequence analysis of pepV, a carnosinase gene from Lactobacillus delbrueckii subsp. lactis DSM 7290, and partial characterization of the enzyme." Microbiology 140:2591-2600(1994). PubMed=7528082 [ 6] Rawlings N.D., Barrett A.J. "Evolutionary families of metallopeptidases." Methods Enzymol. 248:183-228(1995). PubMed=7674922 [E1] https://www.uniprot.org/docs/peptidas -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}