EzCatDB: D00434
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DB codeD00434
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.80

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,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

Enzyme Name
UniProtKBKEGG

P00776
Protein nameStreptogrisin-Astreptogrisin A
Streptomyces griseus protease A
protease A
proteinase A
Streptomyces griseus proteinase A
Streptomyces griseus serine proteinase 3
Streptomyces griseus serine proteinase A
SynonymsEC 3.4.21.80
Serine protease A
SGPA
Pronase enzyme A
MEROPSS01.261 (Serine)
PfamPF02983 (Pro_Al_protease)
PF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberP00776
Entry namePRTA_STRGR
ActivityHydrolysis of proteins with specificity similar to chymotrypsin.
SubunitMonomer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00012C00017C00001C00012C00017I00087I00085I00086
CompoundPeptideProteinH2OPeptideProteinPeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein


ChEBI

15377





PubChem

962
22247451





                
1sgcA01 UnboundUnboundUnboundUnboundUnboundUnboundUnbound
2sgaA01 UnboundUnboundUnboundUnboundUnboundUnboundUnbound
3sgaE01 UnboundUnboundUnboundUnboundUnboundUnboundUnbound
4sgaE01 UnboundUnboundUnboundUnboundUnboundUnboundUnbound
5sgaE01 UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1sgcA02 UnboundUnboundUnboundUnboundUnboundUnboundTransition-state-analogue:CST
2sgaA02 UnboundUnboundUnboundUnboundUnboundUnboundUnbound
3sgaE02 UnboundUnboundUnboundUnboundUnboundIntermediate-bound:PHA-PRO-ALA-PRO-ACE(chain P)Unbound
4sgaE02 UnboundUnboundBound:PHE-PRO-ALA-PRO-ACE(chain P)UnboundUnboundUnboundUnbound
5sgaE02 UnboundUnboundBound:TYR-PRO-ALA-PRO-ACE(chain P)UnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00776 & literature;[6]
pdbCatalytic residuesMain-chain involved in catalysis
          
1sgcA01HIS  57;ASP 102
 
2sgaA01HIS  57;ASP 102
 
3sgaE01HIS  57;ASP 102
 
4sgaE01HIS  57;ASP 102
 
5sgaE01HIS  57;ASP 102
 
1sgcA02SER 195
GLY 193;SER 195
2sgaA02SER 195
GLY 193;SER 195
3sgaE02SER 195
GLY 193;SER 195
4sgaE02SER 195
GLY 193;SER 195
5sgaE02SER 195
GLY 193;SER 195

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.1, p.78-856
[4]p.102-103

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID79050558
PubMed ID101674
JournalJ Mol Biol
Year1978
Volume124
Pages261-83
AuthorsBrayer GD, Delbaere LT, James MN
TitleMolecular structure of crystalline Streptomyces griseus protease A at 2.8 A resolution. II. Molecular conformation, comparison with alpha-chymotrypsin and active-site geometry.
Related UniProtKBP00776
[2]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
Medline ID80140489
PubMed ID119870
JournalJ Mol Biol
Year1979
Volume134
Pages781-804
AuthorsSielecki AR, Hendrickson WA, Broughton CG, Delbaere LT, Brayer GD, James MN
TitleProtein structure refinement: Streptomyces griseus serine protease A at 1.8 A resolution.
Related UniProtKBP00776
[3]
CommentsX-ray crystallography
PubMed ID6783761
JournalJ Mol Biol
Year1980
Volume144
Pages43-88
AuthorsJames MN, Sielecki AR, Brayer GD, Delbaere LT, Bauer CA
TitleStructures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 A resolution. A model for serine protease catalysis.
Related PDB3sga,4sga,5sga
[4]
CommentsX-ray crystallography
PubMed ID3892018
JournalJ Mol Biol
Year1985
Volume183
Pages89-103
AuthorsDelbaere LT, Brayer GD
TitleThe 1.8 A structure of the complex between chymostatin and Streptomyces griseus protease A. A model for serine protease catalytic tetrahedral intermediates.
Related PDB1sgc
[5]
PubMed ID3900416
JournalJ Mol Biol
Year1985
Volume184
Pages479-502
AuthorsFujinaga M, Delbaere LT, Brayer GD, James MN
TitleRefined structure of alpha-lytic protease at 1.7 A resolution. Analysis of hydrogen bonding and solvent structure.
[6]
CommentsX-ray crystallography
PubMed ID3892015
JournalJ Mol Biol
Year1985
Volume182
Pages555-66
AuthorsMoult J, Sussman F, James MN
TitleElectron density calculations as an extension of protein structure refinement. Streptomyces griseus protease A at 1.5 A resolution.
Related PDB2sga
[7]
PubMed ID1744078
JournalJ Biol Chem
Year1991
Volume266
Pages22851-7
AuthorsNebes VL, Jones EW
TitleActivation of the proteinase B precursor of the yeast Saccharomyces cerevisiae by autocatalysis and by an internal sequence.
[8]
PubMed ID8415632
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages8920-4
AuthorsKitson DH, Avbelj F, Moult J, Nguyen DT, Mertz JE, Hadzi D, Hagler AT
TitleOn achieving better than 1-A accuracy in a simulation of a large protein: Streptomyces griseus protease A.
[9]
PubMed ID8119298
JournalEur J Biochem
Year1994
Volume220
Pages55-61
AuthorsKitadokoro K, Tsuzuki H, Nakamura E, Sato T, Teraoka H
TitlePurification, characterization, primary structure, crystallization and preliminary crystallographic study of a serine proteinase from Streptomyces fradiae ATCC 14544.
[10]
PubMed ID7925392
JournalEur J Biochem
Year1994
Volume224
Pages735-42
AuthorsKitadokoro K, Tsuzuki H, Okamoto H, Sato T
TitleCrystal structure analysis of a serine proteinase from Streptomyces fradiae at 0.16-nm resolution and molecular modeling of an acidic-amino-acid-specific proteinase.
[11]
PubMed ID8057380
JournalJ Mol Biol
Year1994
Volume241
Pages574-87
AuthorsBlanchard H, James MN
TitleA crystallographic re-investigation into the structure of Streptomyces griseus proteinase A reveals an acyl-enzyme intermediate.

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.

createdupdated
2004-01-172011-02-21


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