ID M4GGR6_9PEZI Unreviewed; 699 AA.
AC M4GGR6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
OS Mycothermus thermophilus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Mycothermus.
OX NCBI_TaxID=85995 {ECO:0000313|PDB:4AUL};
RN [1] {ECO:0000313|PDB:4AUL, ECO:0007829|PDB:4AUL}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HEME.
RX PubMed=23519415; DOI=10.1107/S0907444912049001;
RA Yuzugullu Y., Trinh C.H., Smith M.A., Pearson A.R., Phillips S.E.,
RA Sutay Kocabas D., Bakir U., Ogel Z.B., McPherson M.J.;
RT "Structure, recombinant expression and mutagenesis studies of the catalase
RT with oxidase activity from Scytalidium thermophilum.";
RL Acta Crystallogr. D 69:398-408(2013).
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000256|PIRNR:PIRNR038927};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927}.
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DR PDB; 4AUL; X-ray; 1.50 A; A/B/C/D=1-699.
DR PDBsum; 4AUL; -.
DR AlphaFoldDB; M4GGR6; -.
DR SMR; M4GGR6; -.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004097; F:catechol oxidase activity; IDA:CACAO.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF3; CATALASE B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0000313|PDB:4AUL, ECO:0007829|PDB:4AUL};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927}.
FT DOMAIN 37..424
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT BINDING 80
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0007829|PDB:4AUL"
FT BINDING 120
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0007829|PDB:4AUL"
FT BINDING 161
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0007829|PDB:4AUL"
FT BINDING 169
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0007829|PDB:4AUL"
FT BINDING 370
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /ligand_part_note="axial binding residue"
FT /evidence="ECO:0007829|PDB:4AUL"
FT BINDING 370
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-2"
FT BINDING 374
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0007829|PDB:4AUL"
FT BINDING 377
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0007829|PDB:4AUL"
SQ SEQUENCE 699 AA; 76896 MW; F0F2AC115DBD3893 CRC64;
MTCPFADPAA LYSRQDTTSG QSPLAAYEVD DSTGYLTSDV GGPIQDQTSL KAGIRGPTLL
EDFMFRQKIQ HFDHERVPER AVNARGAGAH GTFTSYADWS NITAASFLNA TGKQTPVFVR
FSTVAGSRGS ADTARDVHGF ATRFYTDEGN FDIVGNNIPV FFIQDAIQFP DLIHSVKPRP
DNEIPQAATA HDSAWDFFSQ QPSTMHTLFW AMSGHGIPRS YRHMDGFGVH TFRFVKDDGS
SKLIKWHFKS RQGKASLVWE EAQVLSGKNA DFHRQDLWDA IESGNGPEWD VCVQIVDESQ
AQAFGFDLLD PTKIIPEEYA PLTKLGLLKL DRNPTNYFAE TEQVMFQPGH IVRGIDFTED
PLLQGRLFSY LDTQLNRNGG PNFEQLPINM PRVPIHNNNR DGAGQMFIHR NKYPYTPNTL
NSGYPRQANQ NAGRGFFTAP GRTASGALVR EVSPTFNDHW SQPRLFFNSL TPVEQQFLVN
AMRFEISLVK SEEVKKNVLT QLNRVSHDVA VRVAAAIGLG APDADDTYYH NNKTAGVSIV
GSGPLPTIKT LRVGILATTS ESSALDQAAQ LRTRLEKDGL VVTVVAETLR EGVDQTYSTA
DATGFDGVVV VDGAAALFAS TASSPLFPTG RPLQIFVDAY RWGKPVGVCG GKSSEVLDAA
DVPEDGDGVY SEESVDMFVE EFEKGLATFR FTDRFALDS
//
