EzCatDB: D00848
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeD00848
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.-

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
UniProtKBKEGG

Q9I8X1P09872
Protein nameSnake venom serine protease Dav-PAProtein C activatorVenome serine protenase I
Venome serine protenase II
SynonymsSVSP
AaV-SP-I
AaV-SP-II
EC 3.4.21.-
EC 3.4.21.-
ACC-C
Snake venom serine protease
SVSP
MEROPSS01.023 (Serine)
S01.466 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]
PF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberQ9I8X1P09872
Entry nameVSP2_AGKACVSPCA_AGKCO
ActivityThrombin-like snake venom serine protease. Possesses amidolytic activities.Anticoagulant serine protease that acts by quickly activating protein C (PC). This activation is thrombomodulin-independent.
Subunit
Monomer.
Subcellular locationSecreted.Secreted.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00393C00001C00290C00952I00087I00085I00086
CompoundFibrinogenH2OFibrinFibrinopeptide APeptidyl-Ser-tetrahedral-intermediate (with previous peptide)Acyl-enzyme(Peptidyl-Ser-acyl group)Peptidyl-Ser-tetrahedral-intermediate
Typepeptide/proteinH2Oamine group,peptide/proteinpeptide/protein


ChEBI
15377
5054




PubChem
962
22247451
439199




               
1op0A01Unbound UnboundUnboundUnboundUnboundUnbound
1op2A01Unbound UnboundUnboundUnboundUnboundUnbound
2aipA01Unbound UnboundUnboundUnboundUnboundUnbound
2aiqA01Unbound UnboundUnboundUnboundUnboundUnbound
1op0A02Unbound UnboundUnboundUnboundUnboundUnbound
1op2A02Unbound UnboundUnboundUnboundUnboundUnbound
2aipA02Unbound UnboundUnboundUnboundUnboundUnbound
2aiqA02Unbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [5] & Swiss-prot;Q9I8X1, P09872
pdbCatalytic residuesMain-chain involved in catalysis
          
1op0A01SER 195
GLY 193;SER 195
1op2A01SER 195
GLY 193;SER 195
2aipA01SER 195
GLY 193;SER 195
2aiqA01SER 195
GLY 193;SER 195
1op0A02HIS 57;ASP 102
 
1op2A02HIS 57;ASP 102
 
2aipA02HIS 57;ASP 102
 
2aiqA02HIS 57;ASP 102
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]Figure 5, p.4505-4508

references
[1]
CommentsPROTEIN SEQUENCE OF 1-63, FUNCTION.
PubMed ID3624272
JournalJ Biol Chem
Year1987
Volume262
Pages12607-13
AuthorsKisiel W, Kondo S, Smith KJ, McMullen BA, Smith LF
TitleCharacterization of a protein C activator from Agkistrodon contortrix contortrix venom.
[2]
PubMed ID12475199
JournalChem Rev
Year2002
Volume102
Pages4501-24
AuthorsHedstrom L
TitleSerine protease mechanism and specificity.
[3]
CommentsPROTEIN SEQUENCE OF 25-64, FUNCTION, CRYSTALLIZATION.
PubMed ID12595722
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages547-50
AuthorsZhu Z, Gong P, Teng M, Niu L
TitlePurification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom.
[4]
PubMed ID15095007
JournalCell Mol Life Sci
Year2004
Volume61
Pages843-56
AuthorsCastro HC, Zingali RB, Albuquerque MG, Pujol-Luz M, Rodrigues CR
TitleSnake venom thrombin-like enzymes: from reptilase to now.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129.
PubMed ID16162508
JournalJ Biol Chem
Year2005
Volume280
Pages39309-15
AuthorsMurakami MT, Arni RK
TitleThrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator.
Related PDB2aip,2aiq
Related UniProtKBP09872
[6]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-258, FUNCTION, ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-44 AND ASN-70.
PubMed ID15632114
JournalJ Biol Chem
Year2005
Volume280
Pages10524-9
AuthorsZhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L
TitleCrystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.
Related PDB1op0,1op2
Related UniProtKBQ9I8X1

comments
This enzyme belongs to peptidase family-S1.
This enzyme originally belonged to E.C. 3.4.21.74.
Since this enzyme has got the same catalytic site as trypsin, it must catalyze the trypsin-like reaction.

createdupdated
2011-04-042012-08-08


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.