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PROSITE documentation PDOC00395

Catalase signatures

Description:

Catalase (EC 1.11.1.6) [1,2,3] is an enzyme, present in all aerobic cells, that decomposes hydrogen peroxide to molecular oxygen and water. 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.

A conserved tyrosine serves as the heme proximal side ligand. We have used the region around this residue as a first signature pattern; it also includes a conserved arginine that participates in heme-binding. A conserved histidine has been shown to be important for the catalytic mechanism of the enzyme. We have used the region around this residue as a second signature pattern.

Note:

Some prokaryotic catalases belong to the peroxidase family (see <PDOC00394>).

Last update:

December 2001 / Patterns and text revised.

Technical section:

PROSITE methods (with tools and information) covered by this documentation:

CATALASE_1, PS00437; Catalase proximal heme-ligand signature  (PATTERN)
Consensus pattern: R - [LIVMFSTAN] - F - [GASTNP] - Y - x - D - [AST] - [QEH]
Y is the proximal heme-binding ligand
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00437
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00437
• Scan Swiss-Prot/TrEMBL entries against PS00437
• view ligand binding statistics
Matching PDB structures: 1A4E 1CF9 1DGB 1DGF ... [ALL]
CATALASE_2, PS00438; Catalase proximal active site signature  (PATTERN)
Consensus pattern: [IF] - x - [RH] - x(4) - [EQ] - R - x(2) - H - x(2) - [GAS] - [GASTFY] - [GAST]
H is an active site residue
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00438
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00438
• Scan Swiss-Prot/TrEMBL entries against PS00438
• view ligand binding statistics
Matching PDB structures: 1A4E 1CF9 1DGB 1DGF ... [ALL]

References:

1 AuthorsMurthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G.
TitleStructure of beef liver catalase.
SourceJ. Mol. Biol. 152:465-499(1981).
PubMed ID7328661
2 AuthorsMelik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V., Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.
SourceJ. Mol. Biol. 188:63-72(1986).
3 Authorsvon Ossowki I., Hausner G., Loewen P.C.
SourceJ. Mol. Evol. 37:71-76(1993).

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