putative acetylornithine deacetylase (argE)/succinyl-diaminopimelate desuccinylase (dapE) [Candidatus Sulcia muelleri GWSS]
Protein Classification
M20 family metallo-hydrolase( domain architecture ID 10145326)
M20 family metallo-hydrolase similar to the acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like family of enzymes that catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+)
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| M20_ArgE_DapE-like | cd05651 | M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-352 | 0e+00 | ||||||
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: 576.57 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| M20_ArgE_DapE-like | cd05651 | M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-352 | 0e+00 | ||||||
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: 576.57 E-value: 0e+00
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-355 | 3.01e-65 | ||||||
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: 211.28 E-value: 3.01e-65
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| PRK08651 | PRK08651 | succinyl-diaminopimelate desuccinylase; Reviewed |
14-353 | 1.04e-35 | ||||||
succinyl-diaminopimelate desuccinylase; Reviewed Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 133.96 E-value: 1.04e-35
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| DapE-ArgE | TIGR01910 | acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
14-342 | 3.95e-30 | ||||||
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: 118.27 E-value: 3.95e-30
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| Peptidase_M20 | pfam01546 | Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
70-354 | 1.16e-28 | ||||||
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: 113.21 E-value: 1.16e-28
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| Name | Accession | Description | Interval | E-value | ||||||
| M20_ArgE_DapE-like | cd05651 | M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-352 | 0e+00 | ||||||
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: 576.57 E-value: 0e+00
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-355 | 3.01e-65 | ||||||
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: 211.28 E-value: 3.01e-65
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| M20_ArgE_DapE-like | cd08659 | Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
15-352 | 4.71e-65 | ||||||
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: 210.23 E-value: 4.71e-65
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| PRK08651 | PRK08651 | succinyl-diaminopimelate desuccinylase; Reviewed |
14-353 | 1.04e-35 | ||||||
succinyl-diaminopimelate desuccinylase; Reviewed Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 133.96 E-value: 1.04e-35
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| DapE-ArgE | TIGR01910 | acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
14-342 | 3.95e-30 | ||||||
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: 118.27 E-value: 3.95e-30
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| Peptidase_M20 | pfam01546 | Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
70-354 | 1.16e-28 | ||||||
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: 113.21 E-value: 1.16e-28
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| M20_ArgE_LysK | cd05653 | M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
14-352 | 5.93e-28 | ||||||
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: 111.67 E-value: 5.93e-28
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| M20_ArgE_DapE-like | cd08011 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-348 | 1.35e-25 | ||||||
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: 105.55 E-value: 1.35e-25
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| M20_ArgE | cd03894 | M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
16-352 | 3.39e-24 | ||||||
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: 101.90 E-value: 3.39e-24
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| PRK13004 | PRK13004 | YgeY family selenium metabolism-linked hydrolase; |
10-354 | 1.36e-23 | ||||||
YgeY family selenium metabolism-linked hydrolase; Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 100.40 E-value: 1.36e-23
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| M20_ArgE_DapE-like | cd05649 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-352 | 2.12e-22 | ||||||
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: 96.72 E-value: 2.12e-22
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| M20_DapE_proteobac | cd03891 | M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
14-259 | 2.97e-20 | ||||||
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: 90.64 E-value: 2.97e-20
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| PRK08588 | PRK08588 | succinyl-diaminopimelate desuccinylase; Reviewed |
10-355 | 3.92e-20 | ||||||
succinyl-diaminopimelate desuccinylase; Reviewed Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 90.33 E-value: 3.92e-20
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| M20_ArgE_DapE-like | cd05650 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-341 | 3.19e-18 | ||||||
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: 84.82 E-value: 3.19e-18
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| PRK08652 | PRK08652 | acetylornithine deacetylase; Provisional |
12-342 | 1.14e-17 | ||||||
acetylornithine deacetylase; Provisional Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 82.89 E-value: 1.14e-17
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| PRK07522 | PRK07522 | acetylornithine deacetylase; Provisional |
69-251 | 1.21e-17 | ||||||
acetylornithine deacetylase; Provisional Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 83.31 E-value: 1.21e-17
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| M20_ArgE_DapE-like_fungal | cd05652 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-251 | 1.82e-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. 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: 79.24 E-value: 1.82e-16
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| M20_DapE_actinobac | cd05647 | M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
14-251 | 3.37e-16 | ||||||
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. 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 proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE. Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 78.64 E-value: 3.37e-16
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| PRK13983 | PRK13983 | M20 family metallo-hydrolase; |
7-216 | 3.76e-16 | ||||||
M20 family metallo-hydrolase; Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 78.74 E-value: 3.76e-16
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| PRK00466 | PRK00466 | acetyl-lysine deacetylase; Validated |
9-352 | 3.17e-13 | ||||||
acetyl-lysine deacetylase; Validated Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 69.81 E-value: 3.17e-13
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| PRK08737 | PRK08737 | acetylornithine deacetylase; Provisional |
69-251 | 1.06e-11 | ||||||
acetylornithine deacetylase; Provisional Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 65.22 E-value: 1.06e-11
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| M20_ArgE_DapE-like | cd08013 | M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
68-252 | 4.72e-11 | ||||||
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: 63.26 E-value: 4.72e-11
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| PRK06915 | PRK06915 | peptidase; |
10-199 | 1.91e-10 | ||||||
peptidase; Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 61.63 E-value: 1.91e-10
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| PRK13009 | PRK13009 | succinyl-diaminopimelate desuccinylase; Reviewed |
14-259 | 9.40e-10 | ||||||
succinyl-diaminopimelate desuccinylase; Reviewed Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 59.33 E-value: 9.40e-10
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| M20_ArgE_DapE-like | cd03895 | M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-259 | 1.73e-09 | ||||||
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: 58.86 E-value: 1.73e-09
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| M20_dimer | pfam07687 | Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
171-259 | 5.63e-09 | ||||||
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. 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: 400158 [Multi-domain] Cd Length: 107 Bit Score: 53.12 E-value: 5.63e-09
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| M20_CPDG2 | cd03885 | M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
14-251 | 8.75e-09 | ||||||
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: 56.44 E-value: 8.75e-09
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| M20_Acy1 | cd03886 | M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
184-252 | 5.26e-08 | ||||||
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay. Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 54.14 E-value: 5.26e-08
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| M20_dipept_Sso-CP2 | cd05681 | uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
14-140 | 1.88e-07 | ||||||
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: 52.34 E-value: 1.88e-07
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| M20_18_42 | cd18669 | M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
68-166 | 1.02e-06 | ||||||
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: 48.58 E-value: 1.02e-06
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| M20_Dipept_like | cd03893 | M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
17-140 | 2.31e-06 | ||||||
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: 48.86 E-value: 2.31e-06
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| PRK08596 | PRK08596 | acetylornithine deacetylase; Validated |
10-114 | 6.99e-06 | ||||||
acetylornithine deacetylase; Validated Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 47.73 E-value: 6.99e-06
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| M20_PepV | cd03888 | M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
9-254 | 8.08e-06 | ||||||
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: 47.24 E-value: 8.08e-06
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| amidohydrolases | TIGR01891 | amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
165-252 | 8.81e-06 | ||||||
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 46.95 E-value: 8.81e-06
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| M20_PAAh_like | cd03896 | M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
69-353 | 1.10e-05 | ||||||
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: 46.71 E-value: 1.10e-05
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| PRK13013 | PRK13013 | acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
71-166 | 3.92e-05 | ||||||
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 45.14 E-value: 3.92e-05
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| Zinc_peptidase_like | cd03873 | Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
63-166 | 1.10e-04 | ||||||
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: 42.80 E-value: 1.10e-04
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| M20_Acy1_YxeP-like | cd05669 | M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
131-252 | 1.28e-04 | ||||||
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs. Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 43.44 E-value: 1.28e-04
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| M20_dipept_dapE | cd05682 | uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
55-156 | 4.54e-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. This family includes dapE (Lpg0809) from Legionella pneumophila. Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 41.94 E-value: 4.54e-04
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| AbgB | COG1473 | Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
185-252 | 7.43e-04 | ||||||
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 41.26 E-value: 7.43e-04
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| PRK06133 | PRK06133 | glutamate carboxypeptidase; Reviewed |
10-251 | 1.95e-03 | ||||||
glutamate carboxypeptidase; Reviewed Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 40.00 E-value: 1.95e-03
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| PRK08554 | PRK08554 | peptidase; Reviewed |
69-145 | 2.19e-03 | ||||||
peptidase; Reviewed Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 39.76 E-value: 2.19e-03
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| PRK07907 | PRK07907 | hypothetical protein; Provisional |
68-150 | 2.88e-03 | ||||||
hypothetical protein; Provisional Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 39.50 E-value: 2.88e-03
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| M20_peptT_like | cd05683 | M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
20-341 | 3.57e-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: 3.57e-03
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| PRK07338 | PRK07338 | hydrolase; |
69-251 | 6.02e-03 | ||||||
hydrolase; Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 38.41 E-value: 6.02e-03
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| PRK06446 | PRK06446 | hypothetical protein; Provisional |
68-140 | 7.58e-03 | ||||||
hypothetical protein; Provisional Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 38.20 E-value: 7.58e-03
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| M20_yscS | cd05674 | M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
69-258 | 8.39e-03 | ||||||
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: 38.01 E-value: 8.39e-03
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