MULTISPECIES: Sapep family Mn(2+)-dependent dipeptidase [Clostridia]
Protein Classification
zinc-binding metallopeptidase family protein( domain architecture ID 56613)
zinc-binding metallopeptidase family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| Zinc_peptidase_like super family | cl14876 | Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
9-464 | 2.04e-144 | |||||||
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). The actual alignment was detected with superfamily member cd03888: Pssm-ID: 472712 [Multi-domain] Cd Length: 449 Bit Score: 420.50 E-value: 2.04e-144
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| Name | Accession | Description | Interval | E-value | ||||||||
| M20_PepV | cd03888 | M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
9-464 | 2.04e-144 | ||||||||
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme. Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 420.50 E-value: 2.04e-144
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| PRK07318 | PRK07318 | dipeptidase PepV; Reviewed |
1-466 | 3.70e-132 | ||||||||
dipeptidase PepV; Reviewed Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 389.97 E-value: 3.70e-132
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| dipeptidaselike | TIGR01887 | dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
13-461 | 1.11e-128 | ||||||||
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific. Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 380.57 E-value: 1.11e-128
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
3-466 | 3.34e-38 | ||||||||
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 143.10 E-value: 3.34e-38
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| Peptidase_M20 | pfam01546 | Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
85-463 | 1.70e-16 | ||||||||
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 80.08 E-value: 1.70e-16
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| Name | Accession | Description | Interval | E-value | ||||||||
| M20_PepV | cd03888 | M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
9-464 | 2.04e-144 | ||||||||
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme. Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 420.50 E-value: 2.04e-144
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| PRK07318 | PRK07318 | dipeptidase PepV; Reviewed |
1-466 | 3.70e-132 | ||||||||
dipeptidase PepV; Reviewed Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 389.97 E-value: 3.70e-132
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| dipeptidaselike | TIGR01887 | dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
13-461 | 1.11e-128 | ||||||||
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific. Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 380.57 E-value: 1.11e-128
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| PRK07205 | PRK07205 | hypothetical protein; Provisional |
10-467 | 1.98e-79 | ||||||||
hypothetical protein; Provisional Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 253.85 E-value: 1.98e-79
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| dipeptidase | TIGR01886 | dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members ... |
9-466 | 2.66e-72 | ||||||||
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members of the larger M25 subfamily of metalloproteases. Two characterized enzymes are included in the seed. One, from Lactococcus lactis has been shown to act on a wide range of dipeptides, but not larger peptides. The enzyme from Lactobacillus delbrueckii was originally characterized as a Xaa-His dipeptidase, specifically a carnosinase (beta-Ala-His) by complementation of an E. coli mutant. Further study, including the crystallization of the enzyme, has shown it to also be a non-specific dipeptidase. This group also includes enzymes from Streptococcus and Enterococcus. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 130941 [Multi-domain] Cd Length: 466 Bit Score: 235.93 E-value: 2.66e-72
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| PRK06156 | PRK06156 | dipeptidase; |
12-461 | 1.51e-44 | ||||||||
dipeptidase; Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 163.22 E-value: 1.51e-44
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
3-466 | 3.34e-38 | ||||||||
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 143.10 E-value: 3.34e-38
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| M20_ArgE_DapE-like | cd08659 | Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
22-451 | 1.06e-23 | ||||||||
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline. Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 101.99 E-value: 1.06e-23
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| PRK13004 | PRK13004 | YgeY family selenium metabolism-linked hydrolase; |
1-464 | 2.05e-21 | ||||||||
YgeY family selenium metabolism-linked hydrolase; Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 95.78 E-value: 2.05e-21
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| DapE-ArgE | TIGR01910 | acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
17-455 | 5.93e-20 | ||||||||
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 91.31 E-value: 5.93e-20
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| PRK08588 | PRK08588 | succinyl-diaminopimelate desuccinylase; Reviewed |
13-450 | 4.77e-19 | ||||||||
succinyl-diaminopimelate desuccinylase; Reviewed Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 88.40 E-value: 4.77e-19
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| M20_Dipept_like | cd03893 | M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
17-165 | 6.38e-18 | ||||||||
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation. Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 85.46 E-value: 6.38e-18
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| PRK06915 | PRK06915 | peptidase; |
9-141 | 4.06e-17 | ||||||||
peptidase; Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 83.20 E-value: 4.06e-17
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| PRK13983 | PRK13983 | M20 family metallo-hydrolase; |
10-179 | 1.23e-16 | ||||||||
M20 family metallo-hydrolase; Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 81.43 E-value: 1.23e-16
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| Peptidase_M20 | pfam01546 | Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
85-463 | 1.70e-16 | ||||||||
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 80.08 E-value: 1.70e-16
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| M20_ArgE_DapE-like | cd08011 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-284 | 1.91e-16 | ||||||||
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE. Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 80.51 E-value: 1.91e-16
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| M20_ArgE_DapE-like | cd05649 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-153 | 3.13e-16 | ||||||||
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE. Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 80.16 E-value: 3.13e-16
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| PRK13013 | PRK13013 | acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
1-155 | 1.55e-14 | ||||||||
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 75.18 E-value: 1.55e-14
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| PRK08651 | PRK08651 | succinyl-diaminopimelate desuccinylase; Reviewed |
9-165 | 2.14e-14 | ||||||||
succinyl-diaminopimelate desuccinylase; Reviewed Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 74.64 E-value: 2.14e-14
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| M20_dipept_like_CNDP | cd05676 | M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
9-139 | 1.38e-13 | ||||||||
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine. Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 72.63 E-value: 1.38e-13
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| M20_ArgE_DapE-like | cd03895 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-140 | 1.55e-13 | ||||||||
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE. Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 71.96 E-value: 1.55e-13
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| PRK06837 | PRK06837 | ArgE/DapE family deacylase; |
1-140 | 2.09e-12 | ||||||||
ArgE/DapE family deacylase; Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 68.49 E-value: 2.09e-12
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| M20_DapE_proteobac | cd03891 | M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
46-128 | 2.74e-12 | ||||||||
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE. Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 67.91 E-value: 2.74e-12
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| PRK08596 | PRK08596 | acetylornithine deacetylase; Validated |
2-155 | 5.38e-12 | ||||||||
acetylornithine deacetylase; Validated Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 67.37 E-value: 5.38e-12
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| M20_ArgE_DapE-like | cd05650 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-188 | 7.69e-12 | ||||||||
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE. Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 66.71 E-value: 7.69e-12
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| M20_yscS | cd05674 | M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
85-129 | 9.13e-12 | ||||||||
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure. Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 66.90 E-value: 9.13e-12
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| PRK13009 | PRK13009 | succinyl-diaminopimelate desuccinylase; Reviewed |
46-120 | 1.03e-11 | ||||||||
succinyl-diaminopimelate desuccinylase; Reviewed Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 66.26 E-value: 1.03e-11
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| M20_like | cd02697 | M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
17-139 | 2.42e-11 | ||||||||
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc. Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 65.27 E-value: 2.42e-11
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| M20_ArgE_LysK | cd05653 | M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
17-464 | 7.89e-11 | ||||||||
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved. Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 63.14 E-value: 7.89e-11
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| PRK08262 | PRK08262 | M20 family peptidase; |
85-134 | 1.35e-10 | ||||||||
M20 family peptidase; Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 63.04 E-value: 1.35e-10
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| M20_yscS_like | cd05675 | M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
83-188 | 4.47e-10 | ||||||||
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 61.61 E-value: 4.47e-10
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| dapE-lys-deAc | TIGR01902 | N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related ... |
18-153 | 7.57e-10 | ||||||||
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related bacterial species contains two characterized enzymes, an deacetylase with specificity for both N-acetyl-ornithine and N-acetyl-lysine from Thermus, which is found within a lysine biosynthesis operon, and a fusion protein with acetyl-glutamate kinase (an enzyme of ornithine biosynthesis) from Lactobacillus. It is possible that all of the sequences within this clade have dual specificity, or that a mix of specificities have evolved within this clade. Pssm-ID: 130957 [Multi-domain] Cd Length: 336 Bit Score: 60.25 E-value: 7.57e-10
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| M20_dipept_like | cd05680 | uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
17-132 | 8.28e-10 | ||||||||
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 60.79 E-value: 8.28e-10
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| M20_ArgE | cd03894 | M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
85-129 | 1.18e-09 | ||||||||
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved. Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 59.91 E-value: 1.18e-09
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| M20_dipept_Sso-CP2 | cd05681 | uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-165 | 1.20e-09 | ||||||||
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus. Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 60.05 E-value: 1.20e-09
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| M20_18_42 | cd18669 | M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
72-177 | 2.13e-09 | ||||||||
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 57.06 E-value: 2.13e-09
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| PRK07907 | PRK07907 | hypothetical protein; Provisional |
1-155 | 2.20e-09 | ||||||||
hypothetical protein; Provisional Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 59.15 E-value: 2.20e-09
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| PRK08554 | PRK08554 | peptidase; Reviewed |
22-155 | 5.92e-09 | ||||||||
peptidase; Reviewed Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 57.86 E-value: 5.92e-09
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| Zinc_peptidase_like | cd03873 | Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
72-176 | 9.78e-09 | ||||||||
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 55.12 E-value: 9.78e-09
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| PRK06446 | PRK06446 | hypothetical protein; Provisional |
13-130 | 2.26e-08 | ||||||||
hypothetical protein; Provisional Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 55.92 E-value: 2.26e-08
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| PRK07522 | PRK07522 | acetylornithine deacetylase; Provisional |
86-137 | 2.27e-08 | ||||||||
acetylornithine deacetylase; Provisional Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 55.97 E-value: 2.27e-08
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| M20_dipept_like_DUG2_type | cd05677 | M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
16-128 | 1.57e-07 | ||||||||
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex. Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 53.50 E-value: 1.57e-07
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| AcOrn-deacetyl | TIGR01892 | acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
20-269 | 1.66e-07 | ||||||||
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 53.29 E-value: 1.66e-07
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| PRK07906 | PRK07906 | hypothetical protein; Provisional |
83-120 | 2.38e-07 | ||||||||
hypothetical protein; Provisional Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 52.93 E-value: 2.38e-07
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| M20_CPDG2 | cd03885 | M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
45-272 | 3.35e-07 | ||||||||
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells. Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 52.21 E-value: 3.35e-07
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| dapE_proteo | TIGR01246 | succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
42-128 | 4.80e-07 | ||||||||
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 51.65 E-value: 4.80e-07
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| PRK04443 | PRK04443 | [LysW]-lysine hydrolase; |
9-171 | 6.72e-07 | ||||||||
[LysW]-lysine hydrolase; Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 51.11 E-value: 6.72e-07
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| M20_PAAh_like | cd03896 | M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
17-168 | 7.62e-07 | ||||||||
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329. Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 50.94 E-value: 7.62e-07
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| PRK06133 | PRK06133 | glutamate carboxypeptidase; Reviewed |
10-261 | 2.43e-06 | ||||||||
glutamate carboxypeptidase; Reviewed Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 49.63 E-value: 2.43e-06
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| Ac-peptdase-euk | TIGR01880 | N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
85-186 | 4.96e-06 | ||||||||
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids. Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 48.63 E-value: 4.96e-06
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| M20_dipept_dapE | cd05682 | uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
77-170 | 6.50e-06 | ||||||||
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila. Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 48.48 E-value: 6.50e-06
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| M20_ArgE_DapE-like | cd08013 | M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
85-141 | 8.00e-06 | ||||||||
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE. Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 47.86 E-value: 8.00e-06
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| PRK08201 | PRK08201 | dipeptidase; |
1-132 | 8.12e-06 | ||||||||
dipeptidase; Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 48.20 E-value: 8.12e-06
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| M20_AcylaseI_like | cd05646 | M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
86-244 | 1.21e-05 | ||||||||
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB. Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 47.27 E-value: 1.21e-05
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| PRK08652 | PRK08652 | acetylornithine deacetylase; Provisional |
20-245 | 2.47e-05 | ||||||||
acetylornithine deacetylase; Provisional Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 46.29 E-value: 2.47e-05
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| PRK00466 | PRK00466 | acetyl-lysine deacetylase; Validated |
85-155 | 3.55e-05 | ||||||||
acetyl-lysine deacetylase; Validated Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 45.93 E-value: 3.55e-05
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| M20_ArgE_DapE-like | cd05651 | M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
85-129 | 7.05e-05 | ||||||||
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE. Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 44.99 E-value: 7.05e-05
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| PRK08737 | PRK08737 | acetylornithine deacetylase; Provisional |
66-142 | 2.52e-04 | ||||||||
acetylornithine deacetylase; Provisional Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 43.27 E-value: 2.52e-04
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| M20_dipept_like | cd05679 | uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
83-165 | 6.16e-04 | ||||||||
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 42.10 E-value: 6.16e-04
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| M20_ArgE-related | cd08012 | M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
72-117 | 3.97e-03 | ||||||||
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved. Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 39.36 E-value: 3.97e-03
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| M20_peptT_like | cd05683 | M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
12-156 | 5.45e-03 | ||||||||
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein. Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 38.97 E-value: 5.45e-03
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| M20_ArgE_DapE-like_fungal | cd05652 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-161 | 6.23e-03 | ||||||||
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE. Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 38.79 E-value: 6.23e-03
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| PRK12892 | PRK12892 | allantoate amidohydrolase; Reviewed |
387-466 | 7.60e-03 | ||||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 38.53 E-value: 7.60e-03
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