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Database: UniProt
Entry: V5FXH9_BYSSN
LinkDB: V5FXH9_BYSSN
Original site: V5FXH9_BYSSN 
ID   V5FXH9_BYSSN            Unreviewed;       488 AA.
AC   V5FXH9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:GAD93337.1};
GN   ORFNames=PVAR5_1946 {ECO:0000313|EMBL:GAD93337.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD93337.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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:GAD93337.1}.
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DR   EMBL; BAUL01000054; GAD93337.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5FXH9; -.
DR   eggNOG; KOG0047; Eukaryota.
DR   HOGENOM; CLU_010645_2_0_1; -.
DR   InParanoid; V5FXH9; -.
DR   OrthoDB; 3198922at2759; -.
DR   Proteomes; UP000018001; 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   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; 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   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:UP000018001}.
FT   DOMAIN          12..400
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         345
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   488 AA;  55208 MW;  A0407111AD85E713 CRC64;
     MASKSNDRPN YTLAEGRPVA DPRSHLQIGR RGGGGLLLLQ DTQLIETLAH FPRERIPERV
     VHAKAAGALG EFEVTHDVSD ITSAAFLNGI GKKTPLLLRI STVGPEKGSA DTVRDVRGWA
     MKLYTEEGNQ DWVFNNTPVF FVRDPIKFPS LNRSHKRHPQ TNLTDATMFW DFHNNSPESI
     HEIMHVFSDR GTPATLRHMD AFSGHTYKFT KPDGSFKYVK IHIKSDLGNK TMTRQEAAKI
     AGEDPDYHTR DLFNAIESGN YPTWTVYAQV MSPEEAENYR WNVFDITKVW PHSDYPLRPI
     GKITLNKNPE NYFEQIEQAA FSPSTMVPGF APSADPLLQA RMFSYPDAAR YRVGTNYQQL
     PTNAPRCPVY SPFQRDGFMS FRGNYGADPN YVGSTTLPLS TRKVEENYHD HWVGEVTAFA
     SEVTDDDFIQ PKMLWDVMGK QPGQQENFVS NVAAHLSGAI PEVQKETIKL FDRVDPEIGR
     RIEKALKE
//
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