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Database: UniProt
Entry: A0A094EHX9_9PEZI
LinkDB: A0A094EHX9_9PEZI
Original site: A0A094EHX9_9PEZI 
ID   A0A094EHX9_9PEZI        Unreviewed;       905 AA.
AC   A0A094EHX9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 18.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=V499_08552 {ECO:0000313|EMBL:KFY71260.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY71260.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY71260.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY71260.1,
RC   ECO:0000313|Proteomes:UP000029295};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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   -!- 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:KFY71260.1}.
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DR   EMBL; JPKB01001320; KFY71260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EHX9; -.
DR   HOGENOM; CLU_014929_0_0_1; -.
DR   Proteomes; UP000029295; 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; 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:SF26; CATALASE 2; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 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|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}.
FT   DOMAIN          15..404
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
SQ   SEQUENCE   905 AA;  100111 MW;  ACFC893BB22BB3B8 CRC64;
     MAHSQNPPVF TLAEARTIGQ PIADPSNSTV LPARFGGGSL ALLQDTLLIE TLAHFNRERI
     PERVVHARAA AAWGEFEVTH DISHLTTAKF LNGIGKKTKV LQRISTVGGA TGSAETVRDV
     RGFSVKFFTE EGNHDIVGND IPVFFVRDPV KFPSLNRSHK KNPRSNTADE TMFWDFHVNN
     QEGVHALMHL FGSRGIPASL RNINGFGVHT YKLVAVDGSF KYCKFHFKPI GGVQNMSPED
     AAKNAGENAD YHTADLFNAI ENGYYPVWTL YVQVMEPKVA ETYPVNIFDI TKTWPHKDFP
     LLPVGNMTLN KNPHNYFEDV EQAAFSPSNM VPGIAVTPDP MLQARMFAYP DAQRYRLGVN
     YQQLASNRAL SRVYTPYERD GAASFNGNYG GEPNYVRSDF TVAKPGQKSI EHDEWAGGKV
     GIHEIPVSDA DFAQATELWN IFGTQPGEQE GFVKNVAGAI QDIPKKLQEG TIAMFSKVHP
     DIGRKLQAEL NSAGKISASA QSQESARSYQ ILIFILNSRI RHVVNTTTNK LAVDSFLFKI
     VIMTKPVGKV KLDTRVAIEG LFTRREVAPP STKMPKRVPR EKMHRREMIW ELIFDVQVSQ
     DRTGIFVAAR PLTPIGIVSG ERCGPRASLP APTVFTGRPL RGTLVISHDK RQEEVFDVVQ
     LTLQGEVQSI IRLSSGSYCK IKKPLILMSS VKVANEFEQI DAEDPHTVTY QTEFFFDIPD
     FTTLPSSHGN NTPKRLPPSM RVVKSNFISA ATAEIHNSGS IAGTCDVTYK IAACVFAGGR
     LKSDASREII LMPIEDKPPP LEPEDFGKEY RLVGATSLRP SWGLRKSLMV VVSSMEPRPL
     TFSNREEGCE STEVLLHLKT EGLSDGNKSR SSDIFFSGRA KGSYVNGRGT AISVGCVEED
     KVRNK
//
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