DB code: D00059

CATH domain 1.20.144.10 : Vanadium-containing Chloroperoxidase; domain 1
1.10.606.10 : Vanadium-containing Chloroperoxidase; domain 2 Catalytic domain
E.C. 1.11.1.10
CSA 1vnc
M-CSA 1vnc
MACiE M0014

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P49053 Vanadium chloroperoxidase
EC 1.11.1.10
Vanadium chloride peroxidase
VCPO
PF01569 (PAP2)
[Graphical View]

KEGG enzyme name
chloride peroxidase
chloroperoxidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P49053 PRXC_CURIN RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O. Secreted. Vanadium.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C06267 C01371 C00698 C00027 C01334 C00001
E.C.
Compound Vanadium RH Cl- H2O2 RCl H2O
Type heavy metal lipid halide others halide H2O
ChEBI 17996
16240
15377
PubChem 312
22326046
784
22247451
962
1idqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1iduA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1vncA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1vneA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1vnfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1vngA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1vnhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1vniA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1vnsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1idqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1iduA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1vncA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1vneA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1vnfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1vngA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1vnhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1vniA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:VO4 Unbound Unbound Unbound Unbound
1vnsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:SO4 Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P49053 & literature [4], [6], [10]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1idqA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1iduA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1vncA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1vneA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1vnfA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1vngA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1vnhA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1vniA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1vnsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1idqA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;HIS 404;ARG 490 HIS 496(Vanadium binding)
1iduA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;HIS 404;ARG 490 HIS 496(Vanadium binding)
1vncA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;HIS 404;ARG 490 HIS 496(Vanadium binding)
1vneA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;HIS 404;ARG 490 HIS 496(Vanadium binding) mutant D292A
1vnfA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;;HIS 404;ARG 490 HIS 496(Vanadium binding) mutant R360A
1vngA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;;ARG 490 HIS 496(Vanadium binding) mutant H404A
1vnhA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;HIS 404;ARG 490 mutant H496A
1vniA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;HIS 404;ARG 490 HIS 496(Vanadium binding)
1vnsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 353;ARG 360;HIS 404;ARG 490 HIS 496(Vanadium binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.395-396
[2]
Fig.7, p.314
[5]
Fig.2a, p.30-31
[6]
Fig.5, p.23825-23826
[8]
Fig.10, p.603-604
[9]
Fig.8, p.11656
[12]
Fig.1, p.294

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID 96133943
PubMed ID 8552646
Journal Proc Natl Acad Sci U S A
Year 1996
Volume 93
Pages 392-6
Authors Messerschmidt A, Wever R
Title X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.
Related PDB 1vnc
Related UniProtKB P49053
[2]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9165086
Journal Biol Chem
Year 1997
Volume 378
Pages 309-15
Authors Messerschmidt A, Prade L, Wever R
Title Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form.
Related PDB 1idu 1idq 1vne 1vnf
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9224681
Journal FEBS Lett
Year 1997
Volume 409
Pages 317-9
Authors Hemrika W, Wever R
Title A new model for the membrane topology of glucose-6-phosphatase: the enzyme involved in von Gierke disease.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 9260289
Journal Protein Sci
Year 1997
Volume 6
Pages 1764-7
Authors Neuwald AF
Title An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10021409
Journal Curr Opin Chem Biol
Year 1999
Volume 3
Pages 28-34
Authors Littlechild J
Title Haloperoxidases and their role in biotransformation reactions.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10446144
Journal J Biol Chem
Year 1999
Volume 274
Pages 23820-7
Authors Hemrika W, Renirie R, Macedo-Ribeiro S, Messerschmidt A, Wever R
Title Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His(496), Lys(353), Arg(360), and Arg(490).
Related PDB
Related UniProtKB
[7]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10499093
Journal J Biol Inorg Chem
Year 1999
Volume 4
Pages 209-19
Authors Macedo-Ribeiro S, Hemrika W, Renirie R, Wever R, Messerschmidt A
Title X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.
Related PDB 1vng 1vnh 1vni 1vns
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10543953
Journal J Mol Biol
Year 1999
Volume 293
Pages 595-611
Authors Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D
Title X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10766783
Journal J Biol Chem
Year 2000
Volume 275
Pages 11650-7
Authors Renirie R, Hemrika W, Wever R
Title Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10843856
Journal J Mol Biol
Year 2000
Volume 299
Pages 1035-49
Authors Isupov MN, Dalby AR, Brindley AA, Izumi Y, Tanabe T, Murshudov GN, Littlechild JA
Title Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11800602
Journal Inorg Chem
Year 2002
Volume 41
Pages 161-3
Authors Kimblin C, Bu X, Butler A
Title Modeling the catalytic site of vanadium bromoperoxidase: synthesis and structural characterization of intramolecularly H-bonded vanadium(V) oxoperoxo complexes, [VO(O(2))((NH)2pyg(2))]K and [VO(O(2))((BrNH)2pyg(2))]K.
Related PDB
Related UniProtKB
[12]
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

Comments

Created Updated
2004-06-21 2009-02-26