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Database: UniProt/TrEMBL
Entry: Q2J8T5_FRACC
LinkDB: Q2J8T5_FRACC
Original site: Q2J8T5_FRACC 
ID   Q2J8T5_FRACC            Unreviewed;       709 AA.
AC   Q2J8T5;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   20-JUN-2018, entry version 91.
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   OrderedLocusNames=Francci3_2949 {ECO:0000313|EMBL:ABD12307.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD12307.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD12307.1, ECO:0000313|Proteomes:UP000001937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3
RC   {ECO:0000313|Proteomes:UP000001937};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CP000249; ABD12307.1; -; Genomic_DNA.
DR   RefSeq; WP_011437335.1; NC_007777.1.
DR   ProteinModelPortal; Q2J8T5; -.
DR   STRING; 106370.Francci3_2949; -.
DR   PeroxiBase; 4060; FspKat01_CcI3.
DR   EnsemblBacteria; ABD12307; ABD12307; Francci3_2949.
DR   GeneID; 32157818; -.
DR   KEGG; fra:Francci3_2949; -.
DR   eggNOG; ENOG4105CH6; Bacteria.
DR   eggNOG; COG0753; LUCA.
DR   HOGENOM; HOG000087851; -.
DR   KO; K03781; -.
DR   OMA; VMWQMSD; -.
DR   OrthoDB; POG091H0424; -.
DR   BioCyc; FSP106370:G1G5U-3051-MONOMER; -.
DR   Proteomes; UP000001937; 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:UP000001937};
KW   Heme {ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-3,
KW   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, ECO:0000313|EMBL:ABD12307.1};
KW   Peroxidase {ECO:0000256|PIRNR:PIRNR038927,
KW   ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:ABD12307.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001937}.
FT   DOMAIN       32    420       Catalase. {ECO:0000259|SMART:SM01060}.
FT   ACT_SITE     79     79       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   ACT_SITE    152    152       {ECO:0000256|PIRSR:PIRSR038927-1}.
FT   METAL       366    366       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038927-2}.
FT   BINDING      76     76       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     116    116       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     165    165       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     362    362       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
FT   BINDING     373    373       Heme. {ECO:0000256|PIRSR:PIRSR038927-3}.
SQ   SEQUENCE   709 AA;  77701 MW;  0FA90245FDA00C56 CRC64;
     MTDPGTSRLP RDDAKQQQLD AVRIGDDGAR MTTDQGIGVE HTDDSLAAGE RGPTLLEDFH
     FREKLTRFDH ERIPERVVHA RGAGAYGYFE AYESLADVTR AHFLGEDGRR TPVFVRFSTV
     GGSRGSADTV RDVRGFAVKF YTEEGNFDLV GNNMPVFFIQ DGIKFPDFVH AVKPEPHNEI
     PQASSAHNTL WDFVSLVPES MHMMMWLMSD RALPRSYRMM QGFGVHTFRF VDAAGQGTFV
     KFHWRPKLGT HSLVWDETQK IAGKDPDFNR RDLWESIENG TFPEWELGVQ LVPESDEHAF
     DFDLLDATKI IPEERVPVRP VGRLVLNRNP GNFFAETEQV AFCVQNVVPG IDFTNDPLLQ
     ARLFSYLDTQ LIRLGGPNFA QLPVNRPVAA VHNNSRDGYG QHRIQQSQTS YFPNSISGGC
     PVLSDPAHGG YVHYAERVDG NTIRKRSESF KDFYSQATLF WNSMSSWERR HIVDAFSFEL
     GKVDYTQIKE RVLGHLAQVD HELAAGVAEN LGLPVPPEST PNHGRSSPAL SQADQPSGVA
     TRRIAVLAAD GVDEVALRSA TAALREQGAI LEVLAPHGGM LATVSGDALP VDRTLVTMSS
     VLYDAVFVAP GERGVTALTH NGEAVHYVGE AYKHAKPIGA VGAGVSLLEI ASLPGARVAD
     QGDAVVSDRG IVTVRDLAGP SVLGDFGSAF ATAVAAHRHF DRALEAVAA
//
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