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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad2cpoa1 All alpha proteins EF Hand-like Cloroperoxidase Cloroperoxidase Cloroperoxidase (Leptoxyphium fumago ) [TaxId: 5474 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyCloroperoxidase8038909 3000251 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyCloroperoxidase8038906 3000251 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AF_UNCLASSIFIEDe2cpoA2 A: alpha arraysX: EF-handH: Cloroperoxidase (From Topology)T: CloroperoxidaseF: F_UNCLASSIFIEDECOD (1.6)
APF01328e2cpoA1 A: alpha arraysX: EF-handH: Cloroperoxidase (From Topology)T: CloroperoxidaseF: PF01328ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.10.489.10 Mainly Alpha Orthogonal Bundle Chloroperoxidase Chloroperoxidase-likeCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF01328Peroxidase, family 2 (Peroxidase_2)Peroxidase, family 2- Family

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
IPR000028ChloroperoxidaseDomain
IPR036851Chloroperoxidase-like superfamilyHomologous Superfamily

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
PCA Parent Component: GLN

RESIDAA0031

PSI-MOD :  2-pyrrolidone-5-carboxylic acid (Gln) MOD:00040 , 2-pyrrolidone-5-carboxylic acid (Glu) MOD:00420

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

ChainsEnzyme NameDescriptionCatalytic Residues
chloride peroxidase (heme dependent)  M-CSA #250

The heme-dependent chloroperoxidase (CPO) is a ~250 residue heme-containing glycoprotein that is secreted by various fungi. It was first identified in Caldariomyces fumago where it catalyses the hydrogen peroxide-dependent chlorination of cyclopentanedione during the biosynthesis of the antibiotic caldarioymcin. As with many of the peroxidases, it also catalyses the iodination and bromination of a wide range of substrates, dehydrogenation reactions, catalyse-type reactions (facilitating the decomposition of hydrogen peroxide to oxygen and water) and P450-like oxygen insertion reactions. The capability of chloroperoxidase to perform these diverse reactions makes it one of the most versatile of all known heme proteins.

Defined by 4 residues: CYS:A-30 [auth A-29]HIS:A-106 [auth A-105]ASP:A-107 [auth A-106]GLU:A-184 [auth A-183]
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