ID   KATG_MYCSM              Reviewed;         740 AA.
AC   P0C580; O05763; Q59557;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   05-MAY-2009, entry version 11.
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;
GN   Name=katG;
OS   Mycobacterium smegmatis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=mc(2)1216;
RA   Engler O., Telenti A.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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       (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; U46844; AAC45275.1; -; Genomic_DNA.
DR   HSSP; Q939D2; 1MWV.
DR   BRENDA; 1.11.1.6; 259.
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    740       Catalase-peroxidase.
FT                                /FTId=PRO_0000055573.
FT   ACT_SITE    114    114       Proton acceptor (By similarity).
FT   METAL       278    278       Iron (heme axial ligand) (By similarity).
FT   SITE        110    110       Transition state stabilizer (By
FT                                similarity).
FT   CROSSLNK    113    237       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-263) (By similarity).
FT   CROSSLNK    237    263       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-113) (By similarity).
SQ   SEQUENCE   740 AA;  81230 MW;  397CF9B5AA7E1AE7 CRC64;
     MPEDRPIEDS PPIGEAQTDA PAGGCPAGFG RIKPPVAGGS NXDWWPNQLN MKILQKNPDV
     INPLDEDFDY RSAVQNLDVD ALRADIVEVM HTSQDWWPAD FGHYGPLFIR MAWHAAGTYR
     VSDGRGGAGA GMQRFAPLNS WPDNASLDKA RRLLWPVKKK YGKNLSWADL IVYAGNVALE
     DMGFRTAGFA FGREDRWEPE EDVYWGPEQE WLDRTKRYTG ERDLENPLAA VQMGLIYVNP
     EGPNGNPDPQ ASAIDIRETF GRMAMNDVET AALIVGGHTF GKTHGNGDAS LVGPEPEAAP
     LEEVGLGWRN PQGTGVGKDA ITSGLEVTWT HTPTKWDNSF LEILYGNEWE LTKSPAGANQ
     WKPKDNGWAN SVPLAHEDGK THPSMLTSDL ALRVDPIYEQ ITRRWLDHPE ELAEEFAKAW
     FKLLHRDMGP VTRYLGPEVP KDTWLWQDNI PAGNDLSDDE VAKLKELIAD SGLTVSQLVS
     TAWKAASTFR SSDLRGGANG GRIRLQPQLG WEANEPDELA QVVRKYEEIQ KASGINVSFA
     DLVVLGGNVG VEKAAKAAGF DVTVPFTPGR GDATQEETDV DSFAYLEPKA DGFRNYLGKG
     SDLPAEFKLI DRANLLGLSA PEMTTLVGGL RVLDVNHGGT KHGVLTDKPG ALTTDFFVNL
     LDMSTAWKPS PADDGTYIGT DRATGSPKWT GTRVDLVFAS NSQLRALAEV YAEDDSKEKF
     VKDFVAAWTK VMDADRFDVA
//