ID   CATE_MYCAV              Reviewed;         706 AA.
AC   P50979;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Catalase HPII;
DE            EC=1.11.1.6;
GN   Name=katE;
OS   Mycobacterium avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8821941; DOI=10.1046/j.1365-2958.1996.352876.x;
RA   Milano A., de Rossi E., Gusberti L., Heym B., Marone P., Riccardi G.;
RT   "The katE gene, which encodes the catalase HPII of Mycobacterium avium.";
RL   Mol. Microbiol. 19:113-123(1996).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
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:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L41246; AAC18407.1; -; Genomic_DNA.
DR   PIR; S70665; S70665.
DR   AlphaFoldDB; P50979; -.
DR   SMR; P50979; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
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   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
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; PTHR42821; 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; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..706
FT                   /note="Catalase HPII"
FT                   /id="PRO_0000084972"
FT   REGION          512..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         365
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:0000250"
SQ   SEQUENCE   706 AA;  78175 MW;  549269AC4F51AECF CRC64;
     MATDHTSDAP DPKQRDLESA RFRRDTGYLT TQQGVRVDHT DDALTVGERG PTLLEDFHAR
     EKITHFDHER IPERVVHARG AGAYGYFEPY DDRLAQYTAA KFLTSPGTRT PVFVRFSTVA
     GSRGSADTVR DVRGFATKFY TEQGNYDLVG NNFPVFFIQD GIKFPVLVHA VKPEPHNEIP
     QAQSAHDTLW DFVSLQPETL HAIMWLMSDR ALPRSYRMMQ GFGVHTFRLV NARGRGTFVK
     FHWKPRLGVH SLIWDECQKI AGKDPDYNRR DLWEAIESGQ YPEWELGVQL VAEDDEFSFD
     FDLLDATKII PEEQVPVLPV GKMVLNRNPD NFFAETEQVA FHTANVVPGI DFTNDPLLQF
     RNFSYLDTQL IRLGGPNFAQ LPVNRPVAQV RTNQHDGYAQ HAIPQGRSSY FKNSIGGGCP
     ALADEDVFRH YTQRVDGQTI GKRAEAFQNH YGQARMFFKS MSPVEAEHIV AAFAFELGKV
     EMPEIRSAVV AQLARVDDQL AAQVAAKLGL PEPPEEQVDE SAPVSPALSQ VTDGGDTIAS
     RRIAVLAADG VDVVGTQRFT ELMEQRGAVV EVLAPVAGGT LAGGSGGELR VDRSFTTMAS
     VLYDAVVVAC GPRSVSTLSD DGYAVHFVTE AYKHLKPIGA YGAGVDLLRK AGIDNRLAED
     TDVLNDQAVV TTKAAADELP ERFAEEFAAA LAQHRCWQRR TDAVPA