ID   CATR_ASPNG              Reviewed;         730 AA.
AC   P55303;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Catalase R;
DE            EC=1.11.1.6;
GN   Name=catR;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7934925; DOI=10.1111/j.1365-2958.1993.tb01228.x;
RA   Fowler T., Rey M.W., Vaha-Vahe P., Power S.D., Berka R.M.;
RT   "The catR gene encoding a catalase from Aspergillus niger: primary
RT   structure and elevated expression through increased gene copy number and
RT   use of a strong promoter.";
RL   Mol. Microbiol. 9:989-998(1993).
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to 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   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; Z23138; CAA80669.1; -; Genomic_DNA.
DR   EMBL; L15474; AAA68206.1; -; Genomic_DNA.
DR   PIR; S37384; S37384.
DR   AlphaFoldDB; P55303; -.
DR   SMR; P55303; -.
DR   STRING; 5061.CADANGAP00000170; -.
DR   PRIDE; P55303; -.
DR   VEuPathDB; FungiDB:An01g01820; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1116766; -.
DR   VEuPathDB; FungiDB:ATCC64974_21640; -.
DR   VEuPathDB; FungiDB:M747DRAFT_281300; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   SABIO-RK; P55303; -.
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   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..730
FT                   /note="Catalase R"
FT                   /id="PRO_0000084916"
FT   REGION          403..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         392
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   730 AA;  80462 MW;  DC901A1272B103DE CRC64;
     MRHFWLLPAV AGIAGAQCPY LSGEMSFTQE QDNAGDTIEV TEQPIDNTLY VNDTGSYMTT
     DFGTPISDQT SLKAGPRGPT LLEDFIFRQK LQRFDHERVP ERVVHARGAG AYGTFKSYAD
     WSNVTAADFL SANDKETPMF CRFSTVVGFR GSVDTARDVH GHACRFYTDE GNYDIVGINF
     APFFIQDAIQ FPDLVHAIKP MPNNEIPQAA TAHTSAWDFF SQQSTALHSA LWLMSGNGIP
     RSFRHMNGYG VHSFRFVAAN GTSKVVRTPW KSQQGVASLV WDEAQAAAGK NSDYHRQDLY
     NAMPNGHYPK YELQAQIMDE ADMLRFGFDL LDPTKLVPEE VVPYTPLGMM ELNANPTNYF
     AEVEQAGFQP GHVVPGIDFT DDPLLQGRLF SYLDTQLTRH GGPNFEQIPV NRPRKPVHNN
     NRDGFGQQQI PTNNWAYTPN SMSNGYPMQA NQTQGHGFFT APYRYASGHL VRQTSPTFND
     HWSQPAMFWN SLIPAEQQMV VNAIVFENSK VNSPHVRKNV VNQLNMVNNN LAVRVARGLG
     LDEPSPNPTY YTSNKTSNVG TFGKPLLSIE GLQVGFLASN SHPESIKQGQ AMAAQFSAAG
     VDLNIVTEAY ADGVNTTYAL SDAIDFDALI IADGVQSLFA SPALANQMNS TATSTLYPPA
     RPFQILVDSF RYGKPVAAVG SGSVALKNAG IDSSRSGVYT GSSETTEKIA KEVLEGLYTF
     RFVDRFALDE