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Database: UniProt
Entry: A0A2S9PTH1_9ACTN
LinkDB: A0A2S9PTH1_9ACTN
Original site: A0A2S9PTH1_9ACTN 
ID   A0A2S9PTH1_9ACTN        Unreviewed;       485 AA.
AC   A0A2S9PTH1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=C6N75_18680 {ECO:0000313|EMBL:PRH77730.1};
OS   Streptomyces solincola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2100817 {ECO:0000313|EMBL:PRH77730.1, ECO:0000313|Proteomes:UP000239322};
RN   [1] {ECO:0000313|EMBL:PRH77730.1, ECO:0000313|Proteomes:UP000239322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST5x {ECO:0000313|EMBL:PRH77730.1,
RC   ECO:0000313|Proteomes:UP000239322};
RA   Tan G.Y.A., Lee Z.Y.;
RT   "Novel Streptomyces sp. from soil.";
RL   Submitted (MAR-2018) 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|ARBA:ARBA00000720,
CC         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}.
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:PRH77730.1}.
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DR   EMBL; PVLV01000285; PRH77730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9PTH1; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000239322; 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; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239322}.
FT   DOMAIN          7..392
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         337
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   485 AA;  53988 MW;  FDE62E6CB62336A7 CRC64;
     MSKRVLTTES GAPVADNQNS ATAGVGGPLL LQDQHLLEKL ARFNRERIPE RVVHARGSGA
     YGYFEVTDDV TAFTKAGFLS EVGKRTDLFL RFSTVADSLG GSDAVRDPRG FAVKFYTEEG
     NYDLVGNNTP VFFIKDPVKF PDFIHSQKRD PFTGRQEPDN VFDFWAHSPE ATHQITWLFG
     DRGIPASYRH MDGFGSHTYQ WTNEAGEAFF VKYHFKTNQG IRCLSAEQAA ETVGADATSH
     QTDLLQAIER GVNPSWTLYV QIMPAAEAAD YRFNPFDLTK VWPHADYPVQ RVGRLVLDRN
     PDNIFAEVEQ AAFSPNNFVP GIGPSPDKML QGRLFAYADA HRYRLGVNHT QLPVNAPKHA
     VVDNYGRDGL MATRYGSRHD KNYEPNSYAG PAQTDVPLSA PLPVNGHTGT HEAPLHVKDD
     HFFQAGELYR LMSEDEKKRL VANLAGGLSQ VSREDVIDKM VSHFAAADPD YGKRVAEAVR
     ALRED
//
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