DB code: D00434
RLCP classification | 1.13.30000.10 : Hydrolysis | |
---|---|---|
CATH domain | 2.40.10.10 : Thrombin, subunit H | Catalytic domain |
2.40.10.10 : Thrombin, subunit H | Catalytic domain | |
E.C. | 3.4.21.80 | |
CSA | ||
M-CSA | ||
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
2.40.10.10 : Thrombin, subunit H | M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00224 D00497 M00217 M00216 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | MEROPS | Pfam |
---|---|---|---|---|
P00776 |
Streptogrisin-A
|
EC
3.4.21.80
Serine protease A SGPA Pronase enzyme A |
S01.261
(Serine)
|
PF02983
(Pro_Al_protease)
PF00089 (Trypsin) [Graphical View] |
KEGG enzyme name |
---|
streptogrisin A
Streptomyces griseus protease A protease A proteinase A Streptomyces griseus proteinase A Streptomyces griseus serine proteinase 3 Streptomyces griseus serine proteinase A |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P00776 | PRTA_STRGR | Hydrolysis of proteins with specificity similar to chymotrypsin. | Monomer. |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | |||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||||||
KEGG-id | C00012 | C00017 | C00001 | C00012 | C00017 | I00087 | I00085 | I00086 | |||||
E.C. | |||||||||||||
Compound | Peptide | Protein | H2O | Peptide | Protein | Peptidyl-tetrahedral intermediate | Acyl-enzyme | Tetrahedral intermediate | |||||
Type | peptide/protein | peptide/protein | H2O | peptide/protein | peptide/protein | ||||||||
ChEBI |
15377 15377 |
||||||||||||
PubChem |
22247451 962 22247451 962 |
||||||||||||
1sgcA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
2sgaA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3sgaE01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
4sgaE01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
5sgaE01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1sgcA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Transition-state-analogue:CST | ||||||
2sgaA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3sgaE02 | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:PHA-PRO-ALA-PRO-ACE (chain P) | Unbound | ||||||
4sgaE02 | Unbound | Unbound | Bound:PHE-PRO-ALA-PRO-ACE (chain P) | Unbound | Unbound | Unbound | Unbound | ||||||
5sgaE02 | Unbound | Unbound | Bound:TYR-PRO-ALA-PRO-ACE (chain P) | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
Swiss-prot;P00776 & literature;[6] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1sgcA01 | HIS 57;ASP 102 | |||||||||
2sgaA01 | HIS 57;ASP 102 | |||||||||
3sgaE01 | HIS 57;ASP 102 | |||||||||
4sgaE01 | HIS 57;ASP 102 | |||||||||
5sgaE01 | HIS 57;ASP 102 | |||||||||
1sgcA02 | SER 195 | GLY 193;SER 195 | ||||||||
2sgaA02 | SER 195 | GLY 193;SER 195 | ||||||||
3sgaE02 | SER 195 | GLY 193;SER 195 | ||||||||
4sgaE02 | SER 195 | GLY 193;SER 195 | ||||||||
5sgaE02 | SER 195 | GLY 193;SER 195 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[3]
|
Fig.1, p.78-85 | 6 |
[4]
|
p.102-103 |
References | |
---|---|
[1] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
Medline ID | 79050558 |
PubMed ID | 101674 |
Journal | J Mol Biol |
Year | 1978 |
Volume | 124 |
Pages | 261-83 |
Authors | Brayer GD, Delbaere LT, James MN |
Title |
Molecular structure of crystalline Streptomyces griseus protease A at 2.8 A resolution. |
Related PDB | |
Related UniProtKB | P00776 |
[2] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
Medline ID | 80140489 |
PubMed ID | 119870 |
Journal | J Mol Biol |
Year | 1979 |
Volume | 134 |
Pages | 781-804 |
Authors | Sielecki AR, Hendrickson WA, Broughton CG, Delbaere LT, Brayer GD, James MN |
Title | Protein structure refinement: Streptomyces griseus serine protease A at 1.8 A resolution. |
Related PDB | |
Related UniProtKB | P00776 |
[3] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 6783761 |
Journal | J Mol Biol |
Year | 1980 |
Volume | 144 |
Pages | 43-88 |
Authors | James MN, Sielecki AR, Brayer GD, Delbaere LT, Bauer CA |
Title |
Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 A resolution. |
Related PDB | 3sga 4sga 5sga |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 3892018 |
Journal | J Mol Biol |
Year | 1985 |
Volume | 183 |
Pages | 89-103 |
Authors | Delbaere LT, Brayer GD |
Title |
The 1.8 A structure of the complex between chymostatin and Streptomyces griseus protease A. |
Related PDB | 1sgc |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3900416 |
Journal | J Mol Biol |
Year | 1985 |
Volume | 184 |
Pages | 479-502 |
Authors | Fujinaga M, Delbaere LT, Brayer GD, James MN |
Title |
Refined structure of alpha-lytic protease at 1.7 A resolution. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 3892015 |
Journal | J Mol Biol |
Year | 1985 |
Volume | 182 |
Pages | 555-66 |
Authors | Moult J, Sussman F, James MN |
Title |
Electron density calculations as an extension of protein structure refinement. |
Related PDB | 2sga |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1744078 |
Journal | J Biol Chem |
Year | 1991 |
Volume | 266 |
Pages | 22851-7 |
Authors | Nebes VL, Jones EW |
Title | Activation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8415632 |
Journal | Proc Natl Acad Sci U S A |
Year | 1993 |
Volume | 90 |
Pages | 8920-4 |
Authors | Kitson DH, Avbelj F, Moult J, Nguyen DT, Mertz JE, Hadzi D, Hagler AT |
Title | On achieving better than 1-A accuracy in a simulation of a large protein: Streptomyces griseus protease A. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8119298 |
Journal | Eur J Biochem |
Year | 1994 |
Volume | 220 |
Pages | 55-61 |
Authors | Kitadokoro K, Tsuzuki H, Nakamura E, Sato T, Teraoka H |
Title |
Purification, |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7925392 |
Journal | Eur J Biochem |
Year | 1994 |
Volume | 224 |
Pages | 735-42 |
Authors | Kitadokoro K, Tsuzuki H, Okamoto H, Sato T |
Title | Crystal structure analysis of a serine proteinase from Streptomyces fradiae at 0.16-nm resolution and molecular modeling of an acidic-amino-acid-specific proteinase. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8057380 |
Journal | J Mol Biol |
Year | 1994 |
Volume | 241 |
Pages | 574-87 |
Authors | Blanchard H, James MN |
Title | A crystallographic re-investigation into the structure of Streptomyces griseus proteinase A reveals an acyl-enzyme intermediate. |
Related PDB | |
Related UniProtKB |
Comments |
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This enzyme belongs to the peptidase family-S2A.
According to the literature [3] & [4], |
Created | Updated |
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2004-01-17 | 2011-02-21 |