ID G8N610_GEOTH Unreviewed; 735 AA.
AC G8N610;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-APR-2013, entry version 10.
DE RecName: Full=Catalase-peroxidase;
DE Short=CP;
DE EC=1.11.1.21;
DE AltName: Full=Peroxidase/catalase;
GN Name=katG; ORFNames=GTCCBUS3UF5_19650;
OS Geobacillus thermoleovorans CCB_US3_UF5.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1111068;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCB_US3_UF5;
RA Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT CCB_US3_UF5.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-
CC spectrum peroxidase activity (By similarity).
CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
CC -!- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer
CC (By similarity).
CC -!- SUBUNIT: Homodimer or homotetramer (By similarity).
CC -!- PTM: The covalent Trp-Tyr-Met adduct is important for the
CC catalase, but not the peroxidase activity of the enzyme (By
CC similarity).
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily.
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DR EMBL; CP003125; AEV19274.1; -; Genomic_DNA.
DR RefSeq; YP_004982374.1; NC_016593.1.
DR EnsemblBacteria; AEV19274; AEV19274; GTCCBUS3UF5_19650.
DR GeneID; 11626185; -.
DR KEGG; gte:GTCCBUS3UF5_19650; -.
DR KO; K03782; -.
DR GO; GO:0004096; F:catalase activity; IEA:HAMAP.
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 HAMAP; MF_01961; Catal_peroxid; 1; -.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Peroxidase_super; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase.
FT ACT_SITE 101 101 Proton acceptor (By similarity).
FT METAL 264 264 Iron (heme axial ligand) (By similarity).
FT SITE 97 97 Transition state stabilizer (By
FT similarity).
FT CROSSLNK 100 223 Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT (with Met-249) (By similarity).
FT CROSSLNK 223 249 Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT (with Trp-100) (By similarity).
SQ SEQUENCE 735 AA; 82988 MW; FB93204A45145EFF CRC64;
MENQNRQNAA QCPFHGSVTN QSSNRTTNKD WWPNQLNLSI LHQHDRKTNP HDEEFNYAEE
FQKLDYWALK EDLRKLMTES QDWWPADYGH YGPLFIRMAW HSAGTYRIGD GRGGASTGTQ
RFAPLNSWPD NANLDKARRL LWPIKKKYGN KISWADLFIL AGNVAIESMG GKTIGFGGGR
VDVWHPEEDV YWGSEKEWLA SERYSGDREL ENPLAAVQMG LIYVNPEGPD GKPDPKAAAR
DIRETFRRMG MNDEETVALI AGGHTFGKAH GAGPATHVGP EPEAAPIEAQ GLGWISSYGK
GKGSDTITSG IEGAWTPTPT QWDTSYFDML FGYDWWLTKS PAGAWQWMAV DPDEKDLAPD
AEDPSKKVPT MMMTTDLALR FDPEYEKIAR RFHQNPEEFA EAFARAWFKL THRDMGPKTR
YLGPEVPKED FIWQDPIPEV DYELTEAEIE EIKAKILNSG LTVSELVKTA WASASTFRNS
DKRGGANGAR IRLAPQKDWE VNEPERLAKV LSVYEDIQRE LPKKVSIADL IVLGGSAAVE
KAARDAGFDV KVPFFPGRGD ATQEQTDVES FAVLEPFADG FRNYQKQEYS VPPEELLVDK
AQLLGLTAPE MTVLVGGLRV LGANYRDLPH GVFTDRIGVL TNDFFVNLLD MNYEWVPTDS
GIYEIRNRKT GEVRWTATRV DLIFGSNSIL RSYAEFYAQD DNQEKFVRDF INAWVKVMNA
DRFDLVKKAR ESVTA
//
