ID   KATG_MYCIT              Reviewed;         746 AA.
AC   Q04657;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   05-MAY-2009, entry version 57.
DE   RecName: Full=Catalase-peroxidase;
DE            Short=CP;
DE            EC=1.11.1.6;
DE            EC=1.11.1.7;
DE   AltName: Full=Peroxidase/catalase;
DE   AltName: Full=Protein Mi85;
GN   Name=katG; Synonyms=Mi85;
OS   Mycobacterium intracellulare.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93123988; PubMed=1336034;
RA   Morris S.L., Nair J., Rouse D.A.;
RT   "The catalase-peroxidase of Mycobacterium intracellulare: nucleotide
RT   sequence analysis and expression in Escherichia coli.";
RL   J. Gen. Microbiol. 138:2363-2370(1992).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-
CC       spectrum peroxidase activity. May play a role in the intracellular
CC       survival of mycobacteria.
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; M86741; AAA25360.1; -; Genomic_DNA.
DR   PIR; A47685; A47685.
DR   HSSP; Q939D2; 1MWV.
DR   PeroxiBase; 2433; MinCP01.
DR   BRENDA; 1.11.1.6; 21314.
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    746       Catalase-peroxidase.
FT                                /FTId=PRO_0000055570.
FT   ACT_SITE    114    114       Proton acceptor (By similarity).
FT   METAL       277    277       Iron (heme axial ligand) (By similarity).
FT   SITE        110    110       Transition state stabilizer (By
FT                                similarity).
FT   CROSSLNK    113    236       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-262) (By similarity).
FT   CROSSLNK    236    262       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-113) (By similarity).
SQ   SEQUENCE   746 AA;  81418 MW;  15F35F7F5028F2B2 CRC64;
     MSSDTSSSRP PQPDSGTASK SESENPAIPS PKPKAHAPLT NRDWWPDQVD VSSLHPHSPL
     SNPLGDDFDY AAEFAKLDVE ALKADMISLM TTSQDWWPAD YGHYGGLFIR MSWHAAGTYR
     IHDGRGGAGQ GMQRFAPLNS WPDNASLDKA RRLLWPIKKK YGNKISWADL ITYAGNVALE
     SMGFKTFGFG FGREDVWEPE EILWGEEEEW LGTDKRYSGE RELAQPYGAT TMGLIYVNPE
     GPEGKPDPIA AAIDIRETFG RMAMNDEETA ALIVGGHSFG KTHGAGDADL VGPEPEAAPI
     EQQGLGWKSS YGTGSGKDAI TSGLEVVWTP TPTKWDNSFL ETLYGYEWEL TKSPAGAWQF
     TAKDGAGAGT IPDPFGGAGR APTMLVTDIS LRESPIYADI TRRWLDHPEE LADAFAKAWY
     KLLHRDMGPI SRYLGPWVAE PQLWQDPVPA VDHELVDDND VAALKKKVLD SGLSIPQLVK
     TAWSAAASYR NTDKRGGANG GRLRLQPQRS WEVNEPSELD KVLPVLEKIQ QDFNASASGG
     KKISLADLIV LAGSAAVEKA AKDAGYEISV HFAPGRTDAS QESTDVESFA VLEPRADGFR
     NYIRPGEKAP LEQLLIERAY LLGVTGPEMT VLVGGLRALG ANHGSSKHGV FTDRPGALTN
     DFFVNLLDMG TEWKASETAE NVYEGRDRAS GALKWTATAN DLVFGSNSVL RGLVEVYAQD
     DAHGKFVEDF VAAWVKVMNS DRFDLK
//