(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIP3_GEOS0

ID   A0A0F6BIP3_GEOS0        Unreviewed;       488 AA.
AC   A0A0F6BIP3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 24.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   OrderedLocusNames=GY4MC1_0460 {ECO:0000313|EMBL:ADP73294.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73294.1};
RN   [1] {ECO:0000313|EMBL:ADP73294.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73294.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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|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|RuleBase:RU000498}.
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DR   EMBL; CP002293; ADP73294.1; -; Genomic_DNA.
DR   RefSeq; WP_003248176.1; NC_014650.1.
DR   EnsemblBacteria; ADP73294; ADP73294; GY4MC1_0460.
DR   GeneID; 29236884; -.
DR   KEGG; gmc:GY4MC1_0460; -.
DR   KO; K03781; -.
DR   OMA; HADFGRM; -.
DR   OrthoDB; 1584770at2; -.
DR   BioCyc; GSP581103:G1GOQ-511-MONOMER; -.
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; -; 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; IPR037060; Catalase_core_sf.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 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; 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;
DR   PRODOM; A0A0F6BIP3.
DR   SWISS-2DPAGE; A0A0F6BIP3.
KW   Heme {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW   Hydrogen peroxide {ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|PIRSR:PIRSR038928-2, ECO:0000256|RuleBase:RU000498};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038928-2,
KW   ECO:0000256|RuleBase:RU000498};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000498,
KW   ECO:0000313|EMBL:ADP73294.1};
KW   Peroxidase {ECO:0000256|RuleBase:RU000498, ECO:0000313|EMBL:ADP73294.1}.
FT   DOMAIN          8..392
FT                   /note="Catalase"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   METAL           338
FT                   /note="Iron (heme axial ligand)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   488 AA;  55516 MW;  B579D1CA38B51F01 CRC64;
     MADTKKLTTS WGAPVGDNQN SITAGNPGPT LIQDVHLIEK LAHFNRERVP ERVVHAKGAG
     AHGYFEVTND MSKYTKAKVF NGVGKRTPVF VRFSTVAGEL GSADTVRDPR GFAVKFYTEE
     GNYDIVGNNT PIFFIRDAIK FPDFIHTQKR DPRTHLKNPT AMWDFWSLSP ESLHQVTYLF
     GDRGIPLTYR HMNGYGSHTF KWVNEKGEAV WVKYHFKTNQ GVKNMDPELA VKIAGENPDY
     HTEDLYNAIE KGDYPSWTLY VQIMPLEDAK TYRFNPFDVT KVWSHKDYPL IEVGRMVLNR
     NPENYFAEVE QATFSPGNLV PGVEPSPDKM LQARLFAYAD AHRYRVGVNH NLLPINRPRV
     EVNNYQRDGF MRFDNNGGGS VNYEPNSFGG PTEVPEHKTT PFPVSGVAES VPYDDDDHYT
     QAGDLYRLMS EEEKARLVKN IVESLKQVTK EEIKLRQIRH FYKADPDYGR RVAEGLGLQI
     PDDVTTNA
//

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