DB code: S00408
| RLCP classification | 1.13.30000.39 : Hydrolysis | |
|---|---|---|
| CATH domain | 3.40.630.20 : Aminopeptidase | Catalytic domain |
| E.C. | 3.4.19.3 | |
| CSA | 1aug | |
| M-CSA | 1aug | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | MEROPS | Pfam | RefSeq |
|---|---|---|---|---|---|
| O07883 |
Pyrrolidone-carboxylate peptidase
|
PGP-I
EC 3.4.19.3 5-oxoprolyl-peptidase Pyroglutamyl-peptidase I |
C15.001
(Cysteine)
|
PF01470
(Peptidase_C15)
[Graphical View] |
|
| O73944 |
Pyrrolidone-carboxylate peptidase
|
EC
3.4.19.3
5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
C15.001
(Cysteine)
|
PF01470
(Peptidase_C15)
[Graphical View] |
NP_579028.1
(Protein)
NC_003413.1 (DNA/RNA sequence) |
| P46107 |
Pyrrolidone-carboxylate peptidase
|
EC
3.4.19.3
5-oxoprolyl-peptidase Pyroglutamyl-peptidase I PGP-I Pyrase |
C15.001
(Cysteine)
|
PF01470
(Peptidase_C15)
[Graphical View] |
| KEGG enzyme name |
|---|
|
pyroglutamyl-peptidase I
5-oxoprolyl-peptidase pyrase pyroglutamate aminopeptidase pyroglutamyl aminopeptidase L-pyroglutamyl peptide hydrolase pyrrolidone-carboxyl peptidase pyrrolidone-carboxylate peptidase pyrrolidonyl peptidase L-pyrrolidonecarboxylate peptidase pyroglutamidase pyrrolidonecarboxylyl peptidase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| O07883 | PCP_THELI | Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro. | Homotetramer. | Cytoplasm. | |
| O73944 | PCP_PYRFU | Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro. | Homotetramer made of two disulfide-linked dimers. | Cytoplasm. | |
| P46107 | PCP_BACAM | Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro. | Homotetramer. | Cytoplasm. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00017 | C00012 | C00001 | C00017 | C00012 | I00153 | I00154 | I00155 | |||||
| E.C. | |||||||||||||
| Compound | Protein | Peptide | H2O | Protein | Peptide | Peptidyl-Cys-tetrahedral-intermediate (with previous peptide) | Acyl-enzyme(Peptidyl-Cys-acyl group) | Peptidyl-Cys-tetrahedral-intermediate | |||||
| Type | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein | ||||||||
| ChEBI |
15377 15377 |
||||||||||||
| PubChem |
22247451 962 22247451 962 |
||||||||||||
| 1a2zA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1a2zB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1a2zC |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1a2zD |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1iofA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1iofB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1iofC |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1iofD |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ioiA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ioiB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ioiC |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1ioiD |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1augA |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1augB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1augC |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1augD |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P46107,PDB;1a2z | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1a2zA |
|
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|
|
GLU 80;ARG 90;CYS 143;HIS 167 | CYS 143 | |||
| 1a2zB |
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GLU 80;ARG 90;CYS 143;HIS 167 | CYS 143 | |||
| 1a2zC |
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GLU 80;ARG 90;CYS 143;HIS 167 | CYS 143 | |||
| 1a2zD |
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GLU 80;ARG 90;CYS 143;HIS 167 | CYS 143 | |||
| 1iofA |
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GLU 79;ARG 89;CYS 142;HIS 166 | CYS 142 | |||
| 1iofB |
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GLU 79;ARG 89;CYS 142;HIS 166 | CYS 142 | |||
| 1iofC |
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GLU 79;ARG 89;CYS 142;HIS 166 | CYS 142 | |||
| 1iofD |
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GLU 79;ARG 89;CYS 142;HIS 166 | CYS 142 | |||
| 1ioiA |
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GLU 79;ARG 89; ;HIS 166 | mutant C142S | |||
| 1ioiB |
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GLU 79;ARG 89; ;HIS 166 | mutant C142S | |||
| 1ioiC |
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GLU 79;ARG 89; ;HIS 166 | mutant C142S | |||
| 1ioiD |
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GLU 79;ARG 89; ;HIS 166 | mutant C142S | |||
| 1augA |
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GLU 81;ARG 91;CYS 144;HIS 168 | CYS 144 | |||
| 1augB |
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GLU 291;ARG 301;CYS 354;HIS 378 | CYS 354 | |||
| 1augC |
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GLU 501;ARG 511;CYS 564;HIS 588 | CYS 564 | |||
| 1augD |
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GLU 711;ARG 721;CYS 774;HIS 798 | CYS 774 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[1]
|
p.240 | |
|
[2]
|
p.405 | |
|
[3]
|
p.111-112 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | X-ray crystallography (1.73 Angstroms) |
| Medline ID | |
| PubMed ID | 10368293 |
| Journal | Structure Fold Des |
| Year | 1999 |
| Volume | 7 |
| Pages | 237-44 |
| Authors | Singleton M, Isupov M, Littlechild J |
| Title | X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis. |
| Related PDB | 1a2z |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | X-ray crystallography (1.6 Angstroms) |
| Medline ID | 99216536 |
| PubMed ID | 10196127 |
| Journal | Structure Fold Des |
| Year | 1999 |
| Volume | 7 |
| Pages | 399-411 |
| Authors | Odagaki Y, Hayashi A, Okada K, Hirotsu K, Kabashima T, Ito K, Yoshimoto T, Tsuru D, Sato M, Clardy J |
| Title | The crystal structure of pyroglutamyl peptidase I from Bacillus amyloliquefaciens reveals a new structure for a cysteine protease. |
| Related PDB | 1aug |
| Related UniProtKB | P46107 |
| [3] | |
| Resource | |
| Comments | X-ray crystallography (wildtype;2.2/mutant;2.7 Angstroms) |
| Medline ID | |
| PubMed ID | 11432786 |
| Journal | J Biochem (Tokyo) |
| Year | 2001 |
| Volume | 130 |
| Pages | 107-18 |
| Authors | Tanaka H, Chinami M, Mizushima T, Ogasahara K, Ota M, Tsukihara T, Yutani K |
| Title |
X-ray crystalline structures of pyrrolidone carboxyl peptidase from a hyperthermophile, |
| Related PDB | 1iof 1ioi |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments |
X-ray crystallography, |
| Medline ID | |
| PubMed ID | 11359794 |
| Journal | J Biol Chem |
| Year | 2001 |
| Volume | 276 |
| Pages | 18557-62 |
| Authors | Ito K, Inoue T, Takahashi T, Huang HS, Esumi T, Hatakeyama S, Tanaka N, Nakamura KT, Yoshimoto T |
| Title | The mechanism of aubstrate eecognition of pyroglutamyl-peptidase I from Bacillus amyloliquefaciens as determined by X-ray crystallography and site-directed mutagenesis. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
The papers [1],[2] & [3] reported on the catalytic triad Cys-His-Glu, According to the literature [2], |
| Created | Updated |
|---|---|
| 2002-09-27 | 2012-10-22 |