DB code: D00143

CATH domain 1.20.90.10 : Phospholipase A2 Catalytic domain
4.10.410.10 : Factor Xa Inhibitor
E.C. 3.1.1.4
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P00617 Phospholipase A2, beta bungarotoxin A1 chain
EC 3.1.1.4
Phosphatidylcholine 2-acylhydrolase
PF00068 (Phospholip_A2_1)
[Graphical View]
P00989 Beta-bungarotoxin B2 chain
None PF00014 (Kunitz_BPTI)
[Graphical View]

KEGG enzyme name
phospholipase A2
lecithinase A
phosphatidase
phosphatidolipase
phospholipase A

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00617 PA21B_BUNMU Phosphatidylcholine + H(2)O = 1- acylglycerophosphocholine + a carboxylate. Heterodimer, disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors. The A1 chain is found in beta-1 and beta-2 bungarotoxins. Secreted. Binds 1 calcium ion (By similarity).
P00989 IVB2_BUNMU Heterodimer, disulfide-linked. The A chains have phospholipase A2 activity and the B chains show homology with the basic protease inhibitors. Secreted.

KEGG Pathways
Map code Pathways E.C.
MAP00564 Glycerophospholipid metabolism
MAP00565 Ether lipid metabolism
MAP00590 Arachidonic acid metabolism
MAP00591 Linoleic acid metabolism
MAP00592 alpha-Linolenic acid metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00076 C00157 C00001 C00060 C04230
E.C.
Compound Calcium phosphatidylcholine H2O Carboxylate 1-Acyl-sn-glycero-3-phosphocholine
Type divalent metal (Ca2+, Mg2+) amine group,carbohydrate,lipid,phosphate group/phosphate ion H2O carboxyl group amine group,carbohydrate,lipid,phosphate group/phosphate ion
ChEBI 29108
29108
15377
15377
PubChem 271
271
22247451
962
22247451
962
1bunA Analogue:_NA_87 Unbound Unbound Unbound
1bunB Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P00617

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1bunA HIS 48;ASP 94 TYR 28;GLY 30;GLY 32;ASP 49(Calcium binding)
1bunB

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments CHARACTERIZATION OF PRESYNAPTIC NEUROTOXINS.
Medline ID 78043174
PubMed ID 303565
Journal Eur J Biochem
Year 1977
Volume 80
Pages 1-12
Authors Abe T, Alema S, Miledi R
Title Isolation and characterization of presynaptically acting neurotoxins from the venom of Bungarus snakes.
Related PDB
Related UniProtKB P00617
[2]
Resource
Comments CHARACTERIZATION OF PHOSPHOLIPASE A2 ACTIVITY.
Medline ID 79088714
PubMed ID 730754
Journal J Biochem (Tokyo)
Year 1978
Volume 84
Pages 1301-8
Authors Kondo K, Toda H, Narita K
Title Characterization of phospholipase A activity of beta1-bungarotoxin from Bungarus multicinctus venom. II. Identification of the histidine residue of beta1-bungarotoxin modified by p-bromophenacyl bromide.
Related PDB
Related UniProtKB P00617
[3]
Resource
Comments
Medline ID
PubMed ID 2590165
Journal Biochem J
Year 1989
Volume 262
Pages 773-9
Authors Chu ST, Chen YH
Title The intrinsic tryptophan fluorescence of beta 1-bungarotoxin and the Ca2+-binding domains of the toxin as probed with Tb3+ luminescence.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 1898340
Journal Biochem J
Year 1991
Volume 278
Pages 481-6
Authors Chu ST, Chen YH
Title Role of the N-terminal region of phospholipase A2 subunit of beta 1-bungarotoxin in the toxin-Ca2+ complex-formation.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1485347
Journal Toxicon
Year 1992
Volume 30
Pages 1501-4
Authors Shina R, Rosenberg P, Condrea E
Title An EDTA.Ca2+ complex inhibits the enzymatic activity but not the lethality of beta-bungarotoxin.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8240282
Journal Biochem J
Year 1993
Volume 295
Pages 713-8
Authors Chu ST, Chu CC, Tseng CC, Chen YH
Title Met-8 of the beta 1-bungarotoxin phospholipase A2 subunit is essential for the phospholipase A2-independent neurotoxic effect.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 7702746
Journal J Protein Chem
Year 1994
Volume 13
Pages 641-8
Authors Chang LS, Kuo KW, Lin SR, Chang CC
Title Functional involvement of Lys-6 in the enzymatic activity of phospholipase A2 from Bungarus multicinctus (Taiwan banded krait) snake venom.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8060495
Journal J Protein Chem
Year 1994
Volume 13
Pages 233-6
Authors Chang LS, Lin SR, Chang CC, Yang CC
Title The essentiality of B chain in stabilizing the structure of the A chain in beta 1-bungarotoxin from Bungarus multicinctus venom.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8590005
Journal Structure
Year 1995
Volume 3
Pages 1109-19
Authors Kwong PD, McDonald NQ, Sigler PB, Hendrickson WA
Title Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action.
Related PDB 1bun
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8829622
Journal Biochem Mol Biol Int
Year 1996
Volume 38
Pages 617-23
Authors Chang LS, Wen EY, Chang CC
Title The structural elements of phospholipase A2 affecting the enhancement of 8-anilinonaphthalene-1-sulfonate fluorescence.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9161720
Journal Biochem Mol Biol Int
Year 1997
Volume 41
Pages 1247-53
Authors Chang LS, Chang CC, Wu PF
Title The structural and functional essentiality of the N-terminal alpha-helix in the phospholipase A2 of the Taiwan banded krait.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11286555
Journal J Mol Biol
Year 2001
Volume 307
Pages 1049-59
Authors Singh G, Gourinath S, Sharma S, Paramasivam M, Srinivasan A, Singh TP
Title Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.
Related PDB
Related UniProtKB
[13]
Resource
Comments REVIEW.
Medline ID 20396379
PubMed ID 10936627
Journal Toxicon
Year 2001
Volume 39
Pages 107-18
Authors Rowan EG
Title What does beta-bungarotoxin do at the neuromuscular junction?
Related PDB
Related UniProtKB P00617 P00989

Comments
This protein, beta-bungarotoxin, is one of snake venom toxin. It is composed of a phospholipase A2 subunit (A chain) and a smaller Kunitz-type protease inhibitor-like subunit (B chain), which are coupled covalently through a disulfide bond (see [9]).

Created Updated
2004-11-19 2009-02-26