DB code: S00344

CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 1.11.1.10
CSA 1a7u
M-CSA 1a7u
MACiE M0248

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00544 S00517 S00525 S00526 S00720 S00723 S00724 S00725 S00919 S00057 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS
P49323 Non-heme chloroperoxidase
EC 1.11.1.10
Chloride peroxidase
Chloroperoxidase L
CPO-L
S33.992 (Serine)
O31158 Non-heme chloroperoxidase
EC 1.11.1.10
Chloride peroxidase
Chloroperoxidase F
CPO-F
O31168 Non-heme chloroperoxidase
EC 1.11.1.10
Chloride peroxidase
Chloroperoxidase T
CPO-T
S33.991 (Serine)

KEGG enzyme name
chloride peroxidase
chloroperoxidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P49323 PRXC_STRLI RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O. Homodimer.
O31158 PRXC_PSEFL RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O. Homodimer.
O31168 PRXC_STRAU RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O. Homodimer.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C01371 C00698 C00027 C01334 C00001
E.C.
Compound RH Cl- H2O2 RCl H2O
Type lipid halide others halide H2O
ChEBI 17996
 17996
 		16240
 16240
 		15377
 15377
PubChem 312
 312
 		22326046
 784
 22326046
 784
 		22247451
 962
 22247451
 962
1a88A Unbound Unbound Unbound Unbound
1a88B Unbound Unbound Unbound Unbound
1a88C Unbound Unbound Unbound Unbound
1a8sA Bound:PPI Unbound Unbound Unbound
1a7uA Unbound Unbound Unbound Unbound
1a7uB Unbound Unbound Unbound Unbound
1a8uA Bound:BEZ Unbound Unbound Unbound
1a8uB Bound:BEZ Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1a7u, 1a88, 1a8q, 1a8s, 1a8u, 1brt & Swiss-prot;P33912, P29715, O31158, O31168, P49323

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1a88A SER 96;ASP 226;HIS 255
1a88B SER 96;ASP 226;HIS 255
1a88C SER 96;ASP 226;HIS 255
1a8sA SER 94;ASP 224;HIS 253
1a7uA SER 98;ASP 228;HIS 257
1a7uB SER 98;ASP 228;HIS 257
1a8uA SER 98;ASP 228;HIS 257
1a8uB SER 98;ASP 228;HIS 257

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
p.535-536
[3]
p.155-156
[4]
Fig.5, p.895-898
[5]
p.222
[7]
Fig. 5
[8]
Figure 3
[9]
FIGURE 1a

References
[1]
Resource
Comments
Medline ID
PubMed ID 786162
Journal Annu Rev Biochem
Year 1976
Volume 45
Pages 861-88
Authors Morrison M, Schonbaum GR
Title Peroxidase-catalyzed halogenation.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
Medline ID 95393196
PubMed ID 7664081
Journal Nat Struct Biol
Year 1994
Volume 1
Pages 532-7
Authors Hecht HJ, Sobek H, Haag T, Pfeifer O, van Pee KH
Title The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.
Related PDB 1bro
Related UniProtKB P29715
[3]
Resource
Comments
Medline ID
PubMed ID 7632719
Journal Biochim Biophys Acta
Year 1995
Volume 1250
Pages 149-57
Authors Pelletier I, Altenbuchner J, Mattes R
Title A catalytic triad is required by the non-heme haloperoxidases to perform halogenation.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
Medline ID 98307994
PubMed ID 9642069
Journal J Mol Biol
Year 1998
Volume 279
Pages 889-900
Authors Hofmann B, Tolzer S, Pelletier I, Altenbuchner J, van Pee KH, Hecht HJ
Title Structural investigation of the cofactor-free chloroperoxidases.
Related PDB 1a7u 1a88 1a8q 1a8s 1a8u 1brt
Related UniProtKB P33912 P29715 O31158 O31168 P49323
[5]
Resource
Comments
Medline ID
PubMed ID 12369917
Journal Curr Protein Pept Sci
Year 2000
Volume 1
Pages 209-35
Authors Holmquist M
Title Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 12447906
Journal J Mol Recognit
Year 2002
Volume 15
Pages 291-6
Authors Littlechild J, Garcia-Rodriguez E, Dalby A, Isupov M
Title Structural and functional comparisons between vanadium haloperoxidase and acid phosphatase enzymes.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 15381402
Journal Bioorg Chem
Year 2004
Volume 32
Pages 367-75
Authors Bugg TD
Title Diverse catalytic activities in the alphabeta-hydrolase family of enzymes: activation of H2O, HCN, H2O2, and O2.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 15803517
Journal Angew Chem Int Ed Engl
Year 2005
Volume 44
Pages 2742-6
Authors Bernhardt P, Hult K, Kazlauskas RJ
Title Molecular basis of perhydrolase activity in serine hydrolases.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 20112920
Journal Biochemistry
Year 2010
Volume 49
Pages 1931-42
Authors Yin de LT, Bernhardt P, Morley KL, Jiang Y, Cheeseman JD, Purpero V, Schrag JD, Kazlauskas RJ
Title Switching catalysis from hydrolysis to perhydrolysis in Pseudomonas fluorescens esterase.
Related PDB 3hea 3hi4
Related UniProtKB P22862

Comments
This enzyme is closely related to arylesterase (EC 3.1.1.2; S00720 in EzCatDB), which has got a classical catalytic triad composed of Ser/His/Asp.

Created Updated
2004-07-13 2012-03-28