DB code: D00848

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.-
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 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
Q9I8X1 Snake venom serine protease Dav-PA
SVSP
AaV-SP-I
AaV-SP-II
EC 3.4.21.-
S01.023 (Serine)
PF00089 (Trypsin)
[Graphical View]
P09872 Protein C activator
EC 3.4.21.-
ACC-C
Snake venom serine protease
SVSP
S01.466 (Serine)
PF00089 (Trypsin)
[Graphical View]

KEGG enzyme name
Venome serine protenase I
Venome serine protenase II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P09872 VSPCA_AGKCO Anticoagulant serine protease that acts by quickly activating protein C (PC). This activation is thrombomodulin-independent. Monomer. Secreted.
Q9I8X1 VSP2_AGKAC Thrombin-like snake venom serine protease. Possesses amidolytic activities. Secreted.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00393 C00001 C00290 C00952 I00087 I00085 I00086
E.C.
Compound Fibrinogen H2O Fibrin Fibrinopeptide A Peptidyl-Ser-tetrahedral-intermediate (with previous peptide) Acyl-enzyme(Peptidyl-Ser-acyl group) Peptidyl-Ser-tetrahedral-intermediate
Type peptide/protein H2O amine group,peptide/protein peptide/protein
ChEBI 15377
5054
PubChem 22247451
962
439199
1op0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1op2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2aipA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2aiqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1op0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1op2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2aipA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2aiqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Literature [5] & Swiss-prot;Q9I8X1, P09872

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1op0A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1op2A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2aipA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2aiqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1op0A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1op2A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2aipA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2aiqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Figure 5, p.4505-4508

References
[1]
Resource
Comments PROTEIN SEQUENCE OF 1-63, FUNCTION.
Medline ID
PubMed ID 3624272
Journal J Biol Chem
Year 1987
Volume 262
Pages 12607-13
Authors Kisiel W, Kondo S, Smith KJ, McMullen BA, Smith LF
Title Characterization of a protein C activator from Agkistrodon contortrix contortrix venom.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 12475199
Journal Chem Rev
Year 2002
Volume 102
Pages 4501-24
Authors Hedstrom L
Title Serine protease mechanism and specificity.
Related PDB
Related UniProtKB
[3]
Resource
Comments PROTEIN SEQUENCE OF 25-64, FUNCTION, CRYSTALLIZATION.
Medline ID
PubMed ID 12595722
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 547-50
Authors Zhu Z, Gong P, Teng M, Niu L
Title Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 15095007
Journal Cell Mol Life Sci
Year 2004
Volume 61
Pages 843-56
Authors Castro HC, Zingali RB, Albuquerque MG, Pujol-Luz M, Rodrigues CR
Title Snake venom thrombin-like enzymes: from reptilase to now.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS), ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-21; ASN-78 AND ASN-129.
Medline ID
PubMed ID 16162508
Journal J Biol Chem
Year 2005
Volume 280
Pages 39309-15
Authors Murakami MT, Arni RK
Title Thrombomodulin-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 PDB 2aip 2aiq
Related UniProtKB P09872
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-258, FUNCTION, ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-44 AND ASN-70.
Medline ID
PubMed ID 15632114
Journal J Biol Chem
Year 2005
Volume 280
Pages 10524-9
Authors Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L
Title Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases.
Related PDB 1op0 1op2
Related UniProtKB Q9I8X1

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.

Created Updated
2011-04-04 2018-04-23