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Database: UniProt
Entry: A0A1D3DN03_9ACTN
LinkDB: A0A1D3DN03_9ACTN
Original site: A0A1D3DN03_9ACTN 
ID   A0A1D3DN03_9ACTN        Unreviewed;       485 AA.
AC   A0A1D3DN03;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=J116_003765 {ECO:0000313|EMBL:OEJ93717.1};
OS   Streptomyces thermolilacinus SPC6.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1306406 {ECO:0000313|EMBL:OEJ93717.1, ECO:0000313|Proteomes:UP000095329};
RN   [1] {ECO:0000313|EMBL:OEJ93717.1, ECO:0000313|Proteomes:UP000095329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPC6 {ECO:0000313|EMBL:OEJ93717.1,
RC   ECO:0000313|Proteomes:UP000095329};
RX   PubMed=23868127;
RA   Chen X., Zhang B., Zhang W., Wu X., Zhang M., Chen T., Liu G., Dyson P.;
RT   "Genome Sequence of Streptomyces violaceusniger Strain SPC6, a Halotolerant
RT   Streptomycete That Exhibits Rapid Growth and Development.";
RL   Genome Announc. 1:0-0(2013).
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:OEJ93717.1}.
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DR   EMBL; ASHX02000001; OEJ93717.1; -; Genomic_DNA.
DR   RefSeq; WP_023590687.1; NZ_ASHX02000001.1.
DR   AlphaFoldDB; A0A1D3DN03; -.
DR   STRING; 1306406.J116_003765; -.
DR   eggNOG; COG0753; Bacteria.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000095329; 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}.
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;  53984 MW;  B85FC3C90FB3E26F CRC64;
     MSKRVLTTES GAPVADNQNS ATAGIGGPLL IQDQHLIEKL ARFNRERIPE RVVHARGSGA
     YGHFEVTDDV TAYTKAAFLS EVGKRTELFT RFSTVADSLG GADAVRDPRG FAVKFYTEEG
     NYDLVGNNTP VFFIKDPIKF PDFIHSQKRD PFTGKQEPDN VWDFWAHSPE ATHQITWLFG
     DRGIPASYRH MNGYGSHTYL WTNADGEAFF VKYHFKTNQG IRCLSAEQAA EVVGTDPTSH
     QTDLLQAIER GVNPSWTLYV QIMPAAETAD YRFNPFDLTK VWPHADYPLR RVGRMVLDRN
     PENVFAEVEQ AAFSPNNFVP GIGPSPDKML QGRLFAYADA HRYRLGVNHT QLPVNAPKAT
     VADNYGRDGL MATRNGSRHD KNYEPNSYAG PSQTDQALSA ALAVSGYTGT HAAPAHVKDD
     DFFQAGELYR LMSAEEKDRL VANIAGSLSQ VSREDVIEKN LAHFHAADPE YGKRVEEAVR
     ALRED
//
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