CATE_MYCAV
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