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
Q9I8X1	VSP2_AGKAC	Thrombin-like snake venom serine protease. Possesses amidolytic activities.		Secreted.
P09872	VSPCA_AGKCO	Anticoagulant serine protease that acts by quickly activating protein C (PC). This activation is thrombomodulin-independent.	Monomer.	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 15377	5054 5054
PubChem							22247451 962 22247451 962	439199 439199
1op0A01						Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1op2A01						Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
2aipA01						Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
2aiqA01						Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1op0A02						Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1op2A02						Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
2aipA02						Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
2aiqA02						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						SER 195			GLY 193;SER 195
1op2A01						SER 195			GLY 193;SER 195
2aipA01						SER 195			GLY 193;SER 195
2aiqA01						SER 195			GLY 193;SER 195
1op0A02						HIS 57;ASP 102
1op2A02						HIS 57;ASP 102
2aipA02						HIS 57;ASP 102
2aiqA02						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	2012-08-08