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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1ipha1 Alpha and beta proteins (a/b) Flavodoxin-like Class I glutamine amidotransferase-like Catalase, C-terminal domain Catalase, C-terminal domain (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Ad1ipha2 Multi-domain proteins (alpha and beta) Heme-dependent catalase-like Heme-dependent catalase-like Heme-dependent catalases Catalase II (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Bd1iphb1 Alpha and beta proteins (a/b) Flavodoxin-like Class I glutamine amidotransferase-like Catalase, C-terminal domain Catalase, C-terminal domain (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Bd1iphb2 Multi-domain proteins (alpha and beta) Heme-dependent catalase-like Heme-dependent catalase-like Heme-dependent catalases Catalase II (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Cd1iphc1 Alpha and beta proteins (a/b) Flavodoxin-like Class I glutamine amidotransferase-like Catalase, C-terminal domain Catalase, C-terminal domain (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Cd1iphc2 Multi-domain proteins (alpha and beta) Heme-dependent catalase-like Heme-dependent catalase-like Heme-dependent catalases Catalase II (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Dd1iphd1 Alpha and beta proteins (a/b) Flavodoxin-like Class I glutamine amidotransferase-like Catalase, C-terminal domain Catalase, C-terminal domain (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)
Dd1iphd2 Multi-domain proteins (alpha and beta) Heme-dependent catalase-like Heme-dependent catalase-like Heme-dependent catalases Catalase II (Escherichia coli ) [TaxId: 562 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyClass I glutamine amidotransferase-like 8038393 3001405 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyHeme-dependent catalase-like 8038396 3001681 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyHeme-dependent catalase-like 8038396 3001681 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyClass I glutamine amidotransferase-like 8038393 3001405 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyHeme-dependent catalase-like 8038396 3001681 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyClass I glutamine amidotransferase-like 8038393 3001405 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyHeme-dependent catalase-like 8038396 3001681 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyClass I glutamine amidotransferase-like 8038393 3001405 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ACatalasee1iphA1 A: beta barrelsX: Barrel domain in heme-dependent catalases (From Topology)H: Barrel domain in heme-dependent catalases (From Topology)T: Barrel domain in heme-dependent catalasesF: CatalaseECOD (1.6)
ACatalase_1e1iphA2 A: alpha bundlesX: First alpha-helical domain in heme-dependent catalases (From Topology)H: First alpha-helical domain in heme-dependent catalases (From Topology)T: First alpha-helical domain in heme-dependent catalasesF: Catalase_1ECOD (1.6)
ACatalase-rele1iphA3 A: alpha bundlesX: Second alpha-helical domain in heme-dependent catalases (From Topology)H: Second alpha-helical domain in heme-dependent catalases (From Topology)T: Second alpha-helical domain in heme-dependent catalasesF: Catalase-relECOD (1.6)
AGATase1_catalasee1iphA4 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: Class I glutamine amidotransferase-likeF: GATase1_catalaseECOD (1.6)
BCatalasee1iphB1 A: beta barrelsX: Barrel domain in heme-dependent catalases (From Topology)H: Barrel domain in heme-dependent catalases (From Topology)T: Barrel domain in heme-dependent catalasesF: CatalaseECOD (1.6)
BCatalase_1e1iphB2 A: alpha bundlesX: First alpha-helical domain in heme-dependent catalases (From Topology)H: First alpha-helical domain in heme-dependent catalases (From Topology)T: First alpha-helical domain in heme-dependent catalasesF: Catalase_1ECOD (1.6)
BCatalase-rele1iphB3 A: alpha bundlesX: Second alpha-helical domain in heme-dependent catalases (From Topology)H: Second alpha-helical domain in heme-dependent catalases (From Topology)T: Second alpha-helical domain in heme-dependent catalasesF: Catalase-relECOD (1.6)
BGATase1_catalasee1iphB4 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: Class I glutamine amidotransferase-likeF: GATase1_catalaseECOD (1.6)
CCatalasee1iphC1 A: beta barrelsX: Barrel domain in heme-dependent catalases (From Topology)H: Barrel domain in heme-dependent catalases (From Topology)T: Barrel domain in heme-dependent catalasesF: CatalaseECOD (1.6)
CCatalase_1e1iphC2 A: alpha bundlesX: First alpha-helical domain in heme-dependent catalases (From Topology)H: First alpha-helical domain in heme-dependent catalases (From Topology)T: First alpha-helical domain in heme-dependent catalasesF: Catalase_1ECOD (1.6)
CCatalase-rele1iphC3 A: alpha bundlesX: Second alpha-helical domain in heme-dependent catalases (From Topology)H: Second alpha-helical domain in heme-dependent catalases (From Topology)T: Second alpha-helical domain in heme-dependent catalasesF: Catalase-relECOD (1.6)
CGATase1_catalasee1iphC4 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: Class I glutamine amidotransferase-likeF: GATase1_catalaseECOD (1.6)
DCatalasee1iphD1 A: beta barrelsX: Barrel domain in heme-dependent catalases (From Topology)H: Barrel domain in heme-dependent catalases (From Topology)T: Barrel domain in heme-dependent catalasesF: CatalaseECOD (1.6)
DCatalase_1e1iphD2 A: alpha bundlesX: First alpha-helical domain in heme-dependent catalases (From Topology)H: First alpha-helical domain in heme-dependent catalases (From Topology)T: First alpha-helical domain in heme-dependent catalasesF: Catalase_1ECOD (1.6)
DCatalase-rele1iphD3 A: alpha bundlesX: Second alpha-helical domain in heme-dependent catalases (From Topology)H: Second alpha-helical domain in heme-dependent catalases (From Topology)T: Second alpha-helical domain in heme-dependent catalasesF: Catalase-relECOD (1.6)
DGATase1_catalasee1iphD4 A: a/b three-layered sandwichesX: Flavodoxin-likeH: Class I glutamine amidotransferase-likeT: Class I glutamine amidotransferase-likeF: GATase1_catalaseECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF18011C-terminal domain found in long catalases (Catalase_C)C-terminal domain found in long catalasesThis domain is found at the C-terminus of a variety of large catalase enzymes from bacteria. Structurally it is related to class I glutamine amidotransferase domains. The precise molecular function of this domain is uncertain.Domain
A, B, C, D
PF06628Catalase-related immune-responsive (Catalase-rel)Catalase-related immune-responsive- Family
A, B, C, D
PF00199Catalase (Catalase)Catalase- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
CATALASE HPII

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

ChainsEnzyme NameDescriptionCatalytic Residues
catalase (HPII)  M-CSA #573

Catalase is a heme containing enzyme which catalyses the breakdown of hydrogen peroxide to water and molecular oxygen. It also has a peroxidase activity where the reduction of hydrogen peroxide is accompanied by the oxidation of another compound. Catalase is present in all aerobic cells. Its main function is to protect cells from the toxic effects of hydrogen peroxide. In eukaryotic organisms and in some prokaryotes catalase is a molecule composed of four identical subunits. Each of the subunits binds one protoheme IX group. Catalase HPII from Escherichia Coli is the largest known catalase. A unique covalent bond between the Cb of the essential Tyr415 and the Nd of His392 has been noted.

Defined by 3 residues: HIS:A-128ASN:A-201HIS:A-392
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