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
PubChem 22247451
962
1sgcA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2sgaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3sgaE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4sgaE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
5sgaE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:CST
2sgaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3sgaE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PHA-PRO-ALA-PRO-ACE (chain P) Unbound
4sgaE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:PHE-PRO-ALA-PRO-ACE (chain P) Unbound Unbound Unbound Unbound
5sgaE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2sgaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
3sgaE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
4sgaE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
5sgaE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgcA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2sgaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
3sgaE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
4sgaE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
5sgaE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain 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. II. Molecular conformation, comparison with alpha-chymotrypsin and active-site geometry.
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. A model for serine protease catalysis.
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. A model for serine protease catalytic tetrahedral intermediates.
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. Analysis of hydrogen bonding and solvent structure.
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. Streptomyces griseus protease A at 1.5 A resolution.
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, characterization, primary structure, crystallization and preliminary crystallographic study of a serine proteinase from Streptomyces fradiae ATCC 14544.
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
This enzyme belongs to the peptidase family-S2A.
According to the literature [3] & [4], the enzyme has got a similar catalytic triad (Ser/His/Asp) to that of trypsin, suggesting a similar mechanism.

Created Updated
2004-01-17 2011-02-21