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Database: UniProt
Entry: A0A072P2P2_9EURO
LinkDB: A0A072P2P2_9EURO
Original site: A0A072P2P2_9EURO 
ID   A0A072P2P2_9EURO        Unreviewed;       583 AA.
AC   A0A072P2P2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:KEF53967.1};
GN   ORFNames=A1O9_09762 {ECO:0000313|EMBL:KEF53967.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF53967.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF53967.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF53967.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:KEF53967.1}.
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DR   EMBL; AMGV01000011; KEF53967.1; -; Genomic_DNA.
DR   RefSeq; XP_013256557.1; XM_013401103.1.
DR   AlphaFoldDB; A0A072P2P2; -.
DR   STRING; 1182545.A0A072P2P2; -.
DR   GeneID; 25284670; -.
DR   VEuPathDB; FungiDB:A1O9_09762; -.
DR   HOGENOM; CLU_010645_0_0_1; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000027920; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
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   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; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF13; CATALASE (EUROFUNG); 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; 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   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   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT   DOMAIN          59..446
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   BINDING         389
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   583 AA;  65813 MW;  9AB7CE3B251F2688 CRC64;
     MAHPMQAVQE LAGAVGADPR PVQRATLFQG LNDGPATLAA RITGVTSGGP REDNAPYHTN
     NDGIPWPTPT HSKTIGGIPV ASDIFLFQKQ QAFNRHKLLE RIVHPCGSGA FGYFETTKDM
     SHLTKAQFLN GVGTRTPIFI RYSTVTLGRE FPDLARNPRG FAVKFYTGEG NYDLVGLNWP
     VFFSRDPMQG PDVIRSQGRR SDNFLLDYNA TFDLLAHTPE ANHAGMMFFS DHGTPDGWHS
     NHGYGCHTFK WVNKDGKFVY IKYHFRADRG QKMLTRQQAI ELSGVNPDYS KQTLWEAIDR
     GDPISYTACV QIMEPAEADP VELGFDPFDV TKVWPREKYP IQEFGKPHVT KNPENYHRDV
     EQAAFSPGAM VPGIEDSPDS LLQFRMFFYR DAQYHRLGST NYHQIPVNCP FMASSMSSLN
     FDGNMRADSN HSKNPDYAPN SYTPLSKFRP DTANAPYEVS DAIMSRKSHF YHEGKLSDYD
     QPRALYEKVM TNTQRDHLHS NTAVMLAHVS DPRIQILYLG QQYCIKPSYA KAIFDLLPEK
     KFDFNEVEKA SKGAEKRTKT PAFLHTDERE RLVGMPVDGG YNL
//
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