ID KATG1_MYCFO Reviewed; 752 AA. AC O08404; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 05-MAY-2009, entry version 58. DE RecName: Full=Catalase-peroxidase 1; DE Short=CP 1; DE EC=1.11.1.6; DE EC=1.11.1.7; DE AltName: Full=Peroxidase/catalase 1; GN Name=katG1; Synonyms=katGI; OS Mycobacterium fortuitum. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1766; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 6841 / DSM 46621 / IFO 13159 / NBRC 13159 / NCTC 10394; RX MEDLINE=98037481; PubMed=9371430; RA Menendez M.C., Ainsa J.A., Martin C., Garcia M.J.; RT "katGI and katGII encode two different catalases-peroxidases in RT Mycobacterium fortuitum."; RL J. Bacteriol. 179:6880-6886(1997). CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad- CC spectrum peroxidase activity. May play a role in the intracellular CC survival of mycobacteria (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 -!- 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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y07865; CAA69192.1; -; Genomic_DNA. DR HSSP; Q939D2; 1MWV. DR PeroxiBase; 2396; MfoCP01. DR BRENDA; 1.11.1.6; 141585. DR GO; GO:0004096; F:catalase activity; IEA:HAMAP. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01961; -; 1. DR InterPro; IPR000763; Catalase_proxase. 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 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 CHAIN 1 752 Catalase-peroxidase 1. FT /FTId=PRO_0000055572. FT ACT_SITE 117 117 Proton acceptor (By similarity). FT METAL 285 285 Iron (heme axial ligand) (By similarity). FT SITE 113 113 Transition state stabilizer (By FT similarity). FT CROSSLNK 116 244 Tryptophyl-tyrosyl-methioninium (Trp-Tyr) FT (with M-270) (By similarity). FT CROSSLNK 244 270 Tryptophyl-tyrosyl-methioninium (Tyr-Met) FT (with W-116) (By similarity). SQ SEQUENCE 752 AA; 83101 MW; B66BAD53DD26E70D CRC64; MPPNTPDASD ARPPQADTET HSHSESENPV IESPKPKAHA PLTNQDWWPD QVDVSRLHKQ PIEGNPLGAG FNYAEEFQKL DVEALRADML ELMTSSQDWW PRDYGTYAGL FIRMSWHAAG TYRIFDGRGG AGQGAQRFAP INSWPDNVSL DKARRLLWPI KQKYGNKISW ADLIIFAGNV ALESAGFKTF GFAFGRQDIW EPEEILWGQE DTWLGTDKRY GGTNDSTNRE LANPYGATTM GLIYVNPEGP EGKPDPLAAA HDIRETFGRM AMNDEETAAL IVGGHTLGKT HGPGPGDLVG PEPEAAPIEQ QGLGWKCAFG SGKGSDTITS GLEVVWTTTP TKWSNSYLEI LYGYEWELTK SPGDAWQFEA KDAEAIIPDP FGGPPRKPTM LVTDISMRVD PIYGPITRRW LEHPEELNEA FAKAWYKLLH RDMGPISRYL GPWIPEPQLW QDPVPDVDHP LVDEQDIAAL KEKLLDSGLS VQQLVKTAWS AAASFRGTDK RGGANGGRLR LQPQRNWEVN EPSELDKALP VLERIAQDFN ASASDGKKIS LADLIVLGGS AAIEKAARDG GYEVKVHFVA GRTDASQENT DVDSFAVLEP RADGFRNFVR PGDKAPLEQL LVDKAYFLNL TAPEMTVLVG GLRALNTNHG GSKHGVFTAN PGALSNDFFV NLLDMSTEWK PSETAENVYE GRDRRTGQTR WTATANDLVF GSNSVLRAVA EVYAQEDNKA KMIEDFVAAW VKVMNNDRFD LD //