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Database: UniProt
Entry: A0A365Z519_9ACTN
LinkDB: A0A365Z519_9ACTN
Original site: A0A365Z519_9ACTN 
ID   A0A365Z519_9ACTN        Unreviewed;       487 AA.
AC   A0A365Z519;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=DEH69_21900 {ECO:0000313|EMBL:RBM11931.1};
OS   Streptomyces sp. PT12.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1510197 {ECO:0000313|EMBL:RBM11931.1, ECO:0000313|Proteomes:UP000252839};
RN   [1] {ECO:0000313|EMBL:RBM11931.1, ECO:0000313|Proteomes:UP000252839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PT12 {ECO:0000313|EMBL:RBM11931.1,
RC   ECO:0000313|Proteomes:UP000252839};
RA   Devaraj K., Tan G.Y.A.;
RT   "Diversity of actinobacteria isolated from Cape Rachado, Malaysia.";
RL   Submitted (MAY-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:RBM11931.1}.
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DR   EMBL; QEST01000184; RBM11931.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365Z519; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000252839; 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:UP000252839}.
FT   DOMAIN          11..395
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         341
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   487 AA;  54157 MW;  27806199E04F8F86 CRC64;
     MTDQIAAGPL TTEAGAPVAD NQNSQSAGVG GPVLIQDQHL IEKLAHFNRE RIPERIVHAR
     GAGAYGTFTV TADVTPYTRA KFLSEIGKET EVFLRFSTVA GNLGSADAVR DPRGFALKFY
     TEEGNYDLVG NNTPIFFIKD AIKFPDFIHT QKRDPYTGSQ EADNVWDFWG LSPESTHQVT
     WLFGDRGIPA SYRHMNGYGS HTFQWTNEAG EAFWVKYHFK TDQGIKNLTA AEAAKLAGED
     ADSHQRDLRT SIENGDFPSW TVQVQIMPVA EAATYRFNPF DLTKVWPHAD YPPIEIGKLE
     LNRNPENIFA EVEQSIFSPH HFVPGIGPSP DKMLQGRLFA YGDAHRYRVG INADHLPVNR
     PHATEARTHG RDGAAYDGRH GGAKNYEPNS FGGPVQTDRP LWEPLAVTGY TGDHVAPSHA
     EDNDFVQAGN LYRLMSDDEK DRLIENLAGF IAQVSRDDIA ERAIENFRKA DEDYGKRLQA
     AVQALRG
//
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