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Database: UniProt
Entry: A0A2R6P0B0_9APHY
LinkDB: A0A2R6P0B0_9APHY
Original site: A0A2R6P0B0_9APHY 
ID   A0A2R6P0B0_9APHY        Unreviewed;       509 AA.
AC   A0A2R6P0B0;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=PHLCEN_2v6158 {ECO:0000313|EMBL:PSR82088.1};
OS   Hermanssonia centrifuga.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Meruliaceae; Hermanssonia.
OX   NCBI_TaxID=98765 {ECO:0000313|EMBL:PSR82088.1, ECO:0000313|Proteomes:UP000186601};
RN   [1] {ECO:0000313|EMBL:PSR82088.1, ECO:0000313|Proteomes:UP000186601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC195 {ECO:0000313|EMBL:PSR82088.1,
RC   ECO:0000313|Proteomes:UP000186601};
RA   Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA   Riley R.;
RT   "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT   centrifuga.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC       serves to protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|RuleBase:RU004142}.
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|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSR82088.1}.
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DR   EMBL; MLYV02000600; PSR82088.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R6P0B0; -.
DR   STRING; 98765.A0A2R6P0B0; -.
DR   Proteomes; UP000186601; Unassembled WGS sequence.
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; cd08157; catalase_fungal; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF62; CATALASE T; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 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; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186601}.
FT   DOMAIN          16..398
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         346
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:PIRSR038928-2"
SQ   SEQUENCE   509 AA;  56948 MW;  15293E381D2E6D21 CRC64;
     MPSKQAIAAQ DNATYTTSSG APVAEPYAIQ RIGLNGPVLI QDFHHIDLLA HFARERIPER
     VVHAKGAGAH GYFEVTHDIS DLTCASLFSK VGTKCPATAR FSTVGGESGS ADTARDPRGF
     AVKLKTDQGN WDIVANNTPV FFLRDPSKFP HFIHTQKRDP QTHLKDADMF WDYLSLNPES
     VHQVMILFSD RGTPDGYHHM HGYSGHTFKF VDSEGKYTYV QIHFRVRGGF KTLTDAQATK
     LAGENAEYGL QTLFEDIEAG NYPTWDVYVQ TMTAEQAEKF RYNILDLTKV WPHGEFPLRP
     IGKLVLDKYP DNYFAEIEQA AFSPSHLVPG VEPSADPVLQ SRLFSYPDTH RHRLGVNYQQ
     LPVNAPVVPV ANFQRDGFMA INNQGTRPNY QSSLVPLTYK PKPYEQVKHE VWLGNANVDL
     SFITELDFEQ PRALWQKVFD DTAKEHFVGN VAGHLGNVKS PIVKARQLSV FANVDQDLSD
     RIAKAIGHPS VKPLSVPPAS EATRFQYKA
//
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