PF18011

C-terminal domain found in long catalases

Pfam entry
Member databasePfam
Pfam typedomain
Short nameCatalase_C
ClanGlutaminase_I
Author Bateman A;0000-0002-6982-4660
Sequence Ontology0000417

Description

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.

References

1. Structure-function relationships in fungal large-subunit catalases. Diaz A, Valdes VJ, Rudino-Pinera E, Horjales E, Hansberg W. J. Mol. Biol. 386, 218-32, (2009). View articlePMID: 19109972

2. An electrical potential in the access channel of catalases enhances catalysis. Chelikani P, Carpena X, Fita I, Loewen PC. J. Biol. Chem. 278, 31290-6, (2003). View articlePMID: 12777389

3. Modulation of heme orientation and binding by a single residue in catalase HPII of Escherichia coli. Jha V, Louis S, Chelikani P, Carpena X, Donald LJ, Fita I, Loewen PC. Biochemistry 50, 2101-10, (2011). View articlePMID: 21332158

4. Post-transcriptional regulator Hfq binds catalase HPII: crystal structure of the complex. Yonekura K, Watanabe M, Kageyama Y, Hirata K, Yamamoto M, Maki-Yonekura S. PLoS ONE 8, e78216, (2013). View articlePMID: 24223139

5. Crystal structure of catalase HPII from Escherichia coli. Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen PC, Fita I. Structure 3, 491-502, (1995). View articlePMID: 7663946

6. Unusual Cys-Tyr covalent bond in a large catalase. Diaz A, Horjales E, Rudino-Pinera E, Arreola R, Hansberg W. J. Mol. Biol. 342, 971-85, (2004). View articlePMID: 15342250

7. Conformational stability and crystal packing: polymorphism in Neurospora crassa CAT-3. Zarate-Romero A, Stojanoff V, Rojas-Trejo SP, Hansberg W, Rudino-Pinera E. Acta Crystallogr Sect F Struct Biol Cryst Commun 69, 753-8, (2013). View articlePMID: 23832201

8. Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli. Mate MJ, Sevinc MS, Hu B, Bujons J, Bravo J, Switala J, Ens W, Loewen PC, Fita I. J. Biol. Chem. 274, 27717-25, (1999). View articlePMID: 10488114

9. Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli. Melik-Adamyan W, Bravo J, Carpena X, Switala J, Mate MJ, Fita I, Loewen PC. Proteins 44, 270-81, (2001). View articlePMID: 11455600

10. Influence of main channel structure on H(2)O(2) access to the heme cavity of catalase KatE of Escherichia coli. Jha V, Chelikani P, Carpena X, Fita I, Loewen PC. Arch. Biochem. Biophys. 526, 54-9, (2012). View articlePMID: 22820098

11. Mutation of Phe413 to Tyr in catalase KatE from Escherichia coli leads to side chain damage and main chain cleavage. Jha V, Donald LJ, Loewen PC. Arch. Biochem. Biophys. 525, 207-14, (2012). View articlePMID: 22172685

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