ID   KATG2_MYCFO             Reviewed;         733 AA.
AC   O08405;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   05-MAY-2009, entry version 51.
DE   RecName: Full=Catalase-peroxidase 2;
DE            Short=CP 2;
DE            EC=1.11.1.6;
DE            EC=1.11.1.7;
DE   AltName: Full=Peroxidase/catalase 2;
GN   Name=katG2; Synonyms=katGII;
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       (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.
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; Y07866; CAA69193.1; -; Genomic_DNA.
DR   HSSP; Q939D2; 1MWV.
DR   PeroxiBase; 3128; MfoCP02.
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; FALSE_NEG.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN         1    733       Catalase-peroxidase 2.
FT                                /FTId=PRO_0000345093.
FT   ACT_SITE    107    107       Proton acceptor (By similarity).
FT   METAL       275    275       Iron (heme axial ligand) (By similarity).
FT   SITE        103    103       Transition state stabilizer (By
FT                                similarity).
FT   CROSSLNK    106    234       Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
FT                                (with M-260) (By similarity).
FT   CROSSLNK    234    260       Tryptophyl-tyrosyl-methioninium (Tyr-Met)
FT                                (with W-106) (By similarity).
SQ   SEQUENCE   733 AA;  80596 MW;  20C8BCB076F9E58F CRC64;
     MAEAETHPPI GESQTEPAES GCPMRIKPPV EGGSNRDWWP NAVNLKILQK NPPAIDPSDE
     GYDSEAVKSL DVEAFQRDFD ELLTNSQDWW PADFGHYGPL FVRMSWHAAG TYRVEDGRGG
     GGRGMQPFAP LNSWPDNVSL DKARRLLWPL KKKYGKQISW SDLIVYSGNR AMEHMGFKTA
     GFAFGRPDYW EPEEDIYWGA EAEWLGSQDR YAGANGDRTK LENPPXXPHM GLIYVNPEGP
     EGNPDYLAAA IDIRETFGRM AMNDIETAAL IVGGHTFGKT HGATDIENGV EPEXXPLEQM
     GLGWANPGLG NDTVSSGLEV TWTQHPTKWD NSFLEILYSN EWELTKSPAG ANQWKPKDNG
     WANSWPMAQG TGKTHPSMLT TDLSMRFDPI YGEITRRWLD HPEELAEEYA KAWFKLIHRD
     MGPVTRYLGP LVPKQTWLWQ DIIPAGKQLS DADVATLKAA IADSGLSIQQ LVNTAWKAAA
     SYRSSDMRGG NGGRIRLQPQ LGWEVNEPEE LAPVIAKLEE IQAASDSGVS FADLVVLGGV
     VGLEKAIKAA GFDVAVPFTS GPRDALQEQT DVDSFAYLEP KGDGFRNFVA KGDSVPAEYR
     LIDRANLLGL SAPQMTVLIG GLRVLGANHG GSELGVLTDK VGQLTNDYFV NLTDMGTKWA
     PAPADDGTYV GTDRATGSPK WTASRVDLLF GSNSQLRALA EVYAEDDSKE KFVKDFVAAW
     TKVMNADRFD LEA
//