Annotations: 1VNC

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1vnca_	All alpha proteins	Acid phosphatase/Vanadium-dependent haloperoxidase	Acid phosphatase/Vanadium-dependent haloperoxidase	Chloroperoxidase	Chloroperoxidase	(Curvularia inaequalis ) [TaxId: 38902 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Acid phosphatase/Vanadium-dependent haloperoxidase	8038498	3001110	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01569	e1vncA3	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: PF01569	ECOD (1.6)
A	PF17897	e1vncA2	A: alpha bundles	X: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	H: Acid phosphatase/Vanadium-dependent haloperoxidase (From Topology)	T: Acid phosphatase/Vanadium-dependent haloperoxidase	F: PF17897	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.144.10	Mainly Alpha	Up-down Bundle	Vanadium-containing Chloroperoxidase	domain 1	CATH (4.3.0)
A	1.10.606.10	Mainly Alpha	Orthogonal Bundle	Vanadium-containing Chloroperoxidase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF17897	Vanadium chloroperoxidase N-terminal domain (VCPO_N)	Vanadium chloroperoxidase N-terminal domain	This is the N-terminal domain found in Vanadium chloroperoxidase proteins found in fungi [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	VANADIUM-CONTAINING CHLOROPEROXIDASE	cation binding ion binding binding metal ion binding small molecule binding peroxidase activity haloperoxidase activity oxidoreductase activity halogenase activity antioxidant activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity, acting on peroxide as acceptor chloride peroxidase activity catalytic activity	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036938	Phosphatidic acid phosphatase type 2/haloperoxidase superfamily	Homologous Superfamily
A	IPR016119	Bromoperoxidase/chloroperoxidase C-terminal	Homologous Superfamily
A	IPR041067	Vanadium chloroperoxidase, N-terminal	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	chloride peroxidase (vanadate dependent) M-CSA #14	Chloride peroxidase oxidises chloride in the presence of hydrogen peroxidase to form hypochlorous acid. This acid is the final product of the reaction in the absence of a suitable nucleophilic acceptor. However, it can go on to form a diversity of halogenated reaction products if a convenient nucleophilic acceptor is present. Hypochlorous acid is strongly bacteriocidal and a powerful oxidising agent. It is secreted by pathogenic fungi e.g. Curvularia inaequalis in a mechanism to oxidise plant cell walls to facilitate penetration of the fungus into the host amongst other uses. It can also act upon Br- and I-.	Defined by 7 residues: LYS:A-353ARG:A-360SER:A-402GLY:A-403HIS:A-404ARG:A-490HIS:A-496 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.11.1.10 (PDB Primary Data) Search M-CSA Motif + EC 1.11.1.10

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.