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Database: UniProt/TrEMBL
Entry: A0A1Y0CF74_9MYCO
LinkDB: A0A1Y0CF74_9MYCO
Original site: A0A1Y0CF74_9MYCO 
ID   A0A1Y0CF74_9MYCO        Unreviewed;       702 AA.
AC   A0A1Y0CF74;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   28-MAR-2018, entry version 7.
DE   RecName: Full=Catalase {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
GN   Name=katE {ECO:0000313|EMBL:ART73910.1};
GN   ORFNames=BTO20_26400 {ECO:0000313|EMBL:ART73910.1};
OS   Mycobacterium dioxanotrophicus.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=482462 {ECO:0000313|EMBL:ART73910.1, ECO:0000313|Proteomes:UP000195331};
RN   [1] {ECO:0000313|EMBL:ART73910.1, ECO:0000313|Proteomes:UP000195331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH-06 {ECO:0000313|EMBL:ART73910.1,
RC   ECO:0000313|Proteomes:UP000195331};
RA   He Y.;
RT   "Whole Genome Sequence of 1,4-Dioxane Degrading Bacterium
RT   Mycobacterium dioxanotrophicus PH-06.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of
CC       hydrogen peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRNR:PIRNR038927,
CC         ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP020809; ART73910.1; -; Genomic_DNA.
DR   KEGG; mdx:BTO20_26400; -.
DR   KO; K03781; -.
DR   Proteomes; UP000195331; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 2.40.180.10; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56634; SSF56634; 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   Complete proteome {ECO:0000313|Proteomes:UP000195331};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|PIRSR:PIRSR038927-2, ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498}.
FT   DOMAIN       25    414       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     72     72       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    146    146       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       360    360       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   702 AA;  77331 MW;  A2CEAD66D36174B1 CRC64;
     MNNTPNPKQQ QLEGARVDNG KGYLTTQQGV RIDHTDDALT AGERGPTLLE DFHAREKVTH
     FDHERIPERV VHARGAGAYG YFEPYDDGLA DFTAAKFLTT PGLRTPVFVR FSTVAGSRGS
     ADTVRDVRGF ATKFYTEQGN YDLVGNNFPV FFIQDGIKFP DFVHAVKPEP HNEIPQAASA
     HNTLWDFVSL QPETLHAIMW LMSDRALPRS YRMMQGFGVH TFRLVNASGQ GVFVKFHWKP
     LLGVHSLIWE ECQQIAGKDP DFNRRDLWEA IEAGHYPEWE LGVQLIPESD EFDFPFDLLD
     ATKIVPEERV PVLPVGRMVL DRNPDNFFAE TEQVAFHTAN LVPGIDFTND PLLQFRNFSY
     LDTQLIRLGG PNFAHLPVNR PIADVRNNQR DGYSQHTIAQ GPTSYYKNTL GGGCPALADE
     DVFRHYTERV DGHKIRRRAE SFKDYYSQPR LFWDSMSAVE AEHIVAAFAF ELGKVGPETG
     IRPRVVEQLN LIDHDLAARV AAKLGLTAPA EVSIDVRHAP SPALSQLNAV PHTIDTRRIA
     VLAAGGVDVR GIERAAAALR RLGATVDIIS TVGGGTVWCD TGHELAVDLG INTTSSALYD
     AVLVPGGAES VEQLTQDGSM IHFVSEAYKH LKPIAAFGAG IDVLQAAGVR TRVANGSGAV
     SDDGVITSRT SGDDLDDAFI GALVGAVERH RVWDRVTDMI PA
//
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