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Database: UniProt/TrEMBL
Entry: A0A1P8Y2Y8_9ACTN
LinkDB: A0A1P8Y2Y8_9ACTN
Original site: A0A1P8Y2Y8_9ACTN 
ID   A0A1P8Y2Y8_9ACTN        Unreviewed;       699 AA.
AC   A0A1P8Y2Y8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   28-MAR-2018, entry version 10.
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:AQA14752.1};
GN   ORFNames=BV401_34415 {ECO:0000313|EMBL:AQA14752.1};
OS   Streptomyces autolyticus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA14752.1, ECO:0000313|Proteomes:UP000187851};
RN   [1] {ECO:0000313|Proteomes:UP000187851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA   Yin M., Jiang M., Lu T.;
RT   "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL   Submitted (JAN-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; CP019458; AQA14752.1; -; Genomic_DNA.
DR   KEGG; sauo:BV401_34415; -.
DR   KO; K03781; -.
DR   Proteomes; UP000187851; 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:UP000187851};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187851}.
FT   DOMAIN       24    411       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     71     71       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    144    144       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       358    358       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   699 AA;  77341 MW;  BAB390E69EC1CD73 CRC64;
     MTEDRKERQR EKYRAADPAE GPLTTDQGVA VDHTDDSLTV GERGPTLMED FHFREKVTHF
     DHERIPERVV HARGAGAYGY FEPYESCAEF TRAAFLQDPS VRTPVFVRFS TVQGPRGSAD
     TVRDVRGFAT KFYTSEGNYD LVGNNMPVFF IQDGIKFPDF VHALKPEPQN EIPTGASAHD
     TLWDFVSLQP ETMHMMMWLM SDRAIPRSFR MMQGFGVHTF RFVDAQGHGT FVKFHWKPKL
     GVHSLVWDEA QECAGRDPDF NRRDLWQAIE AGQYPEYELG VQLVPEEDEF NFDFDLLDAT
     KIIPEEQVPV RPIGHMVLDR NPDNFFAETE QVAFHTGNVV PGIDFTNDPL LQARNFSYLD
     TQLIRLGGPN FSQIPVNQPV APARTNHRDG YHQTMIHKGT SYSPNSLGGG CPALAGADGY
     AFSHYAERVE GHKIRKRSES FKDFYSQAAL FWNSMADWER RHIVEAFQFE LGKVDAVHVR
     ERTVEQLAHV DYDLASQVAQ GIGVARPEPG ANNHKPQASP ALSLDNLHGD GSIRTRQIAV
     LVTDGVDTGQ LAQAQEALTN QGAIVEAIAP HDGKVLGADG NGYAVDRALP TVASVLYDAV
     LLPGGPTGTP ALGSDSAAMR FVRDAYRHGK PIGALGSGVG ILSTLEPEGL HIASGHGHVC
     TDRGVVTDTT TGTASEDFTR AFTEAIAAHR HWNRPPVRC
//
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