ID   F3ZIX7_9ACTN            Unreviewed;       481 AA.
AC   F3ZIX7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=STTU_3991 {ECO:0000313|EMBL:EGJ76780.1};
OS   Streptomyces sp. Tu6071.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ76780.1};
RN   [1] {ECO:0000313|EMBL:EGJ76780.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ76780.1};
RA   Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA   Gunther S.;
RT   "Genome sequence of Streptomyces sp. Tu6071.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CM001165; EGJ76780.1; -; Genomic_DNA.
DR   RefSeq; WP_007825936.1; NZ_CM001165.1.
DR   AlphaFoldDB; F3ZIX7; -.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   Proteomes; UP000003955; Chromosome.
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   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:SF9; CATALASE; 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}.
FT   DOMAIN          7..389
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         336
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   481 AA;  54782 MW;  55AFB3DAA44202CB CRC64;
     MADPISTNNT GIPVESDQYS LSVGPDGPIL LQDNYLIEKM AQFNRERVPE RVVHAKGSGA
     YGTFEVTNDV SQFTRADLFQ PGRRTKMLAR FSTVAGEQGS PDTWRDPRGF ALKFYTQEGV
     YDLVGNNTPI FFMRDPSKFQ DFIRSQKRTI PSALRDNDMQ WDYWTLSPES AHQVTYLMGD
     RGIPKTYRNM NGYGSHTYLW INGAGQRTWV KYHFHSDQGV DHLTDMEAAA MAGEDADHHR
     RDLYDAIERG EAPSWTLYVQ TIPYEDAASY RYNIFDVTKT VPHSDYPLIE VGRMTLHTNP
     TDFFTHIEQA AFDPSDLVPG IGPSPDKMLQ ARLFSYADTH RYRVGTNYTQ LPPNRTINEV
     RSYAKDGAMR YFEPNVARPY APNSYGGPSA DEERWNKPAG WLVDSAEIVR SAYTLHQDDD
     DFSQPGTLVR EVMDDAQRER LVGNVTRHLD NGVSVKVRER AFEYWRNIDP SVGDRIAASF
     G
//