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Database: UniProt
Entry: S7ZQ39_PENO1
LinkDB: S7ZQ39_PENO1
Original site: S7ZQ39_PENO1 
ID   S7ZQ39_PENO1            Unreviewed;       730 AA.
AC   S7ZQ39;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   03-MAY-2023, entry version 41.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE            EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN   ORFNames=PDE_05708 {ECO:0000313|EMBL:EPS30756.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS30756.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS30756.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
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   -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC       peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|PIRNR:PIRNR038927,
CC       ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; KB644412; EPS30756.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7ZQ39; -.
DR   STRING; 933388.S7ZQ39; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_3_0_1; -.
DR   OrthoDB; 3198922at2759; -.
DR   PhylomeDB; S7ZQ39; -.
DR   Proteomes; UP000019376; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
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   Gene3D; 2.40.180.10; Catalase core domain; 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   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42821; CATALASE; 1.
DR   PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT   DOMAIN          34..425
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   BINDING         371
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:PIRSR038927-2"
SQ   SEQUENCE   730 AA;  82106 MW;  96548A7B8A0F771C CRC64;
     MSVQQQIDNA KSGDGKVKDL QKDTYELNDK QHMTTDYGVK ISDPDHWLRV VNEKQTGPML
     LEDQIGREKI MRFDHERIPE RVVHARGTAA FGTFKLFESA EDVTTAGVLT DTSRETPLFL
     RFSTVQGSKG SADTVRDVRG FAVKMYTPEG NWDIVGNNIP VFFIQDAIKF PDVVHSVKPE
     PHNEVPQGQS AHNNFWDFVY MHSETTHMNY WQMSDRAIPR SYRMMQGFGV NTYSLVNKEG
     KRHLVKFHFT PELGVHSLVW DEALKICGQD PDFHRKDLME AIEKGHFPRW KFGLQLIPEE
     KADDFEFDPL DATKVWPEEL VPIRYIGQME LNRNVDEFFP QTEQVAFCTS HIVPGIDFSN
     DPLLQGRNFS YFDTQISRLG PNWQELPINR PVCPYMNLVN RDGQGKHRIT KGTVNYWPNR
     FGTNPPAEPA QGGFTSYPEK IQGTKARLLS EKFKEHYNQA QTFYNSLSQI EKAHVAKAFS
     FELDHCDDPI VYKRMTERIA SISTELAETV ANNVGGDLPS KSPRSNHGKT AKGLSQLEYM
     PEKAVIDTRR VAILIADGFD YDAYTTMKDA LTERGAFVFT IGAQRKGVTS ESGQTVTPDH
     FFVGMRSTLF DATFVPGGKH VAEGLAKSGV AKHWIAEAFS HLKAIAGVNE AVPFIKKQIG
     LDEVKVASPG ASVADSYGVV TGYGDASSTL KVSGEIGPES KGLGEKFIWH ISRHRNWQRE
     LDGLSDQVGA
//
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