Annotations: 1IPH

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ipha1	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)
A	d1ipha2	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)
B	d1iphb1	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)
B	d1iphb2	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)
C	d1iphc1	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)
C	d1iphc2	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)
D	d1iphd1	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)
D	d1iphd2	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

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8038393	3001405	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Heme-dependent catalase-like	8038396	3001681	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Heme-dependent catalase-like	8038396	3001681	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8038393	3001405	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Heme-dependent catalase-like	8038396	3001681	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8038393	3001405	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Heme-dependent catalase-like	8038396	3001681	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Class I glutamine amidotransferase-like	8038393	3001405	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	Catalase	e1iphA1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
A	Catalase_1	e1iphA2	A: alpha bundles	X: 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 catalases	F: Catalase_1	ECOD (1.6)
A	Catalase-rel	e1iphA3	A: alpha bundles	X: 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 catalases	F: Catalase-rel	ECOD (1.6)
A	GATase1_catalase	e1iphA4	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: GATase1_catalase	ECOD (1.6)
B	Catalase	e1iphB1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
B	Catalase_1	e1iphB2	A: alpha bundles	X: 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 catalases	F: Catalase_1	ECOD (1.6)
B	Catalase-rel	e1iphB3	A: alpha bundles	X: 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 catalases	F: Catalase-rel	ECOD (1.6)
B	GATase1_catalase	e1iphB4	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: GATase1_catalase	ECOD (1.6)
C	Catalase	e1iphC1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
C	Catalase_1	e1iphC2	A: alpha bundles	X: 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 catalases	F: Catalase_1	ECOD (1.6)
C	Catalase-rel	e1iphC3	A: alpha bundles	X: 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 catalases	F: Catalase-rel	ECOD (1.6)
C	GATase1_catalase	e1iphC4	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: GATase1_catalase	ECOD (1.6)
D	Catalase	e1iphD1	A: beta barrels	X: Barrel domain in heme-dependent catalases (From Topology)	H: Barrel domain in heme-dependent catalases (From Topology)	T: Barrel domain in heme-dependent catalases	F: Catalase	ECOD (1.6)
D	Catalase_1	e1iphD2	A: alpha bundles	X: 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 catalases	F: Catalase_1	ECOD (1.6)
D	Catalase-rel	e1iphD3	A: alpha bundles	X: 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 catalases	F: Catalase-rel	ECOD (1.6)
D	GATase1_catalase	e1iphD4	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Class I glutamine amidotransferase-like	F: GATase1_catalase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)
A	1.20.1370.20	Mainly Alpha	Up-down Bundle	Hemocyanin, N-terminal domain	Catalase, four-helical domain	CATH (4.3.0)
A	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)
B	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)
B	1.20.1370.20	Mainly Alpha	Up-down Bundle	Hemocyanin, N-terminal domain	Catalase, four-helical domain	CATH (4.3.0)
B	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)
C	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)
C	1.20.1370.20	Mainly Alpha	Up-down Bundle	Hemocyanin, N-terminal domain	Catalase, four-helical domain	CATH (4.3.0)
C	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)
D	2.40.180.10	Mainly Beta	Beta Barrel	Catalase HpII, Chain A, domain 1	Catalase core domain	CATH (4.3.0)
D	1.20.1370.20	Mainly Alpha	Up-down Bundle	Hemocyanin, N-terminal domain	Catalase, four-helical domain	CATH (4.3.0)
D	3.40.50.880	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Class I glutamine amidotransferase (GATase) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF18011	C-terminal domain found in long catalases (Catalase_C)	C-terminal domain found in long catalases	This 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	PF06628	Catalase-related immune-responsive (Catalase-rel)	Catalase-related immune-responsive	-	Family
A, B, C, D	PF00199	Catalase (Catalase)	Catalase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	CATALASE HPII	peroxidase activity oxidoreductase activity antioxidant activity catalase activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding peroxidase activity oxidoreductase activity antioxidant activity catalase activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity binding organic cyclic compound binding tetrapyrrole binding heme binding cation binding transition metal ion binding iron ion binding ion binding metal ion binding small molecule binding identical protein binding protein binding	cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process hydrogen peroxide catabolic process response to oxidative stress response to osmotic stress hyperosmotic response cellular response to stimulus cellular response to stress response to stimulus DNA damage response response to stress cellular process catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process hydrogen peroxide catabolic process response to oxidative stress response to osmotic stress hyperosmotic response response to abiotic stimulus	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR029062	Class I glutamine amidotransferase-like	Homologous Superfamily
A, B, C, D	IPR024708	Catalase active site	Active Site
A, B, C, D	IPR041399	Large catalase, C-terminal domain	Domain
A, B, C, D	IPR010582	Catalase immune-responsive domain	Domain
A, B, C, D	IPR043156	Catalase, mono-functional, haem-containing, clade 2, helical domain	Homologous Superfamily
A, B, C, D	IPR002226	Catalase haem-binding site	Binding Site
A, B, C, D	IPR020835	Catalase superfamily	Homologous Superfamily
A, B, C, D	IPR024712	Catalase, mono-functional, haem-containing, clade 2	Family
A, B, C, D	IPR011614	Catalase core domain	Domain
A, B, C, D	IPR018028	Catalase, mono-functional, haem-containing	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	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 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.11.1.6 (PDB Primary Data) Search M-CSA Motif + EC 1.11.1.6

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.