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Database: UniProt/TrEMBL
Entry: C9ZES1_STRSW
LinkDB: C9ZES1_STRSW
Original site: C9ZES1_STRSW 
ID   C9ZES1_STRSW            Unreviewed;       697 AA.
AC   C9ZES1;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   20-DEC-2017, entry version 59.
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:CBG68854.1};
GN   OrderedLocusNames=SCAB_17231 {ECO:0000313|EMBL:CBG68854.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG68854.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG68854.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG68854.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H.,
RA   Parry R.J., Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like
RT   biosynthetic cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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; FN554889; CBG68854.1; -; Genomic_DNA.
DR   ProteinModelPortal; C9ZES1; -.
DR   STRING; 680198.SCAB_17231; -.
DR   PeroxiBase; 7272; STscKat01.
DR   EnsemblBacteria; CBG68854; CBG68854; SCAB_17231.
DR   KEGG; scb:SCAB_17231; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; POG091H0424; -.
DR   Proteomes; UP000001444; Chromosome.
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   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:UP000001444};
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:UP000001444}.
FT   DOMAIN       22    409       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     69     69       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    142    142       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       356    356       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
SQ   SEQUENCE   697 AA;  76715 MW;  3EDC8F7F108922D4 CRC64;
     MDRKRDQREA AHPDDPASGP LTTDQGVAVD HTDDSLTVGE RGPTLMEDFH FREKLTHFDH
     ERIPERVVHA RGAGAYGYFE PYASCAEFTR AAFLQDPSVR TPVFVRFSTV QGPRGSADTV
     RDVRGFATKF YTSEGNYDLV GNNFPVFFIQ DGIKFPDFVH AVKPEPHNDI PTGASAHDTL
     WDFVSLQPET LHAIMWLMSD RAIPRSYRMM QGFGVHTFRF VTADGRGTFV KFHWKPKLGT
     HALVWDEAQE CQGRDPDFNR RDLWDAIEAG EYPEWELGVQ LVPEEDEFAF DFDLLDATKL
     IPEEQVPVRP IGRMVLDRNP ENFFAETEQV AFHTANVVPG IDFTNDPLLQ ARNFSYLDTQ
     LIRLGGPNFS QLPVNRPVAP VRTNHRDGYH QSAVHGGTNY FPNSLGGGCP AHAGGDPHAY
     RHYAERVDGA TIRRRSESFK DHHSQAALFW NSMAPWEREH IVAAFRFELG KVGALAVRAR
     TVEQLTKVDQ ELAAEVAKGI GVPVPADAGP TPYKLASPAL SLEAQRGPGS IRTRQIAVLV
     SDGVDAQQVT GVREALAAEG AIVEALAARD GTVRGADGAE YTVDRALPTV ASVLYDAVFL
     PGGPVGTPSR AADPDAMRFV RDAYRHGKPI GALGSGVGVV AALRPEGVRL SSEFHHVVAD
     RGVVTDTAQG TAGEDFTREF VAAIAAHRHW DRPPTHC
//
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