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Database: UniProt
Entry: A0A2D0HNL9_9NOSO
LinkDB: A0A2D0HNL9_9NOSO
Original site: A0A2D0HNL9_9NOSO 
ID   A0A2D0HNL9_9NOSO        Unreviewed;       497 AA.
AC   A0A2D0HNL9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=CK516_04610 {ECO:0000313|EMBL:PHM11112.1};
OS   Nostoc sp. 'Peltigera malacea cyanobiont' DB3992.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1206980 {ECO:0000313|EMBL:PHM11112.1, ECO:0000313|Proteomes:UP000223928};
RN   [1] {ECO:0000313|EMBL:PHM11112.1, ECO:0000313|Proteomes:UP000223928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DB3992 {ECO:0000313|EMBL:PHM11112.1};
RA   Gagunashvili A.N., Andresson O.S.;
RT   "Distinctive characters of Nostoc genomes in cyanolichens.";
RL   Submitted (AUG-2017) 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:PHM11112.1}.
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DR   EMBL; NSHF01000025; PHM11112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0HNL9; -.
DR   Proteomes; UP000223928; 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:UP000223928}.
FT   DOMAIN          8..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   REGION          371..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         338
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   497 AA;  56185 MW;  D28CA87F6E19F979 CRC64;
     MTEPQNLTTA DGIPVSDNQN SLTAGARGPV LIQDFHLLEK LAHFNRERIP ERVVHAKGAA
     AHGTLTITND ITRYSKAKLF SEIGKKTELL LRFSTVGGEK GSADAERDPR GFSLKFYTEE
     GNWDLVGNNT PIFFIRDPLK FPDFIHTQKR NPQTNCKDQN AKWDFWSLSP ESLHQVTILF
     SDRGVPKTHR HMDGFGSHTF SLINAEGDRV WCKFHFKTLQ GHQTLTEEES AKIKGEDPDH
     ATHDLFEAIA NKDYPKWRMC IQVMTDEQAA KHPDNPFDLT KVWKQREYPL IEVGILELNR
     NPENYFAEVE QAAFSPSAVV PGISFSPDKM LQARIFSYPD AQRYRLGGNY QQLPVNQPKC
     PVMHYQRDGF MASGNNGGSV PNYEPNSAEG TPKENPAYAE PPSHLGDVTV DRYSHREGND
     DYTQAGNLYR LLTPEQQERL AKNIVGSLSQ AREDIQMRQL CHFFRADISY GRRVAEGLGI
     SIDPSVFSHN AQPVGNW
//
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