ID   KATG_FRATT              Reviewed;         741 AA.
AC   Q5NGV7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
DE   Flags: Precursor;
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=FTT_0721c;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-41, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=NY 96-3369;
RX   PubMed=16790773; DOI=10.1128/iai.00257-06;
RA   Lee B.-Y., Horwitz M.A., Clemens D.L.;
RT   "Identification, recombinant expression, immunolocalization in macrophages,
RT   and T-cell responsiveness of the major extracellular proteins of
RT   Francisella tularensis.";
RL   Infect. Immun. 74:4002-4013(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01961};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC       {ECO:0000255|HAMAP-Rule:MF_01961};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16790773}. Periplasm
CC       {ECO:0000269|PubMed:16790773}. Note=Released by the bacterium
CC       intracellularly in host macrophages.
CC   -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC       for the catalase, but not the peroxidase activity of the enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01961}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR   EMBL; AY662299; AAT77112.1; -; Genomic_DNA.
DR   EMBL; AJ749949; CAG45354.1; -; Genomic_DNA.
DR   RefSeq; WP_003020536.1; NZ_CP010290.1.
DR   RefSeq; YP_169735.1; NC_006570.2.
DR   AlphaFoldDB; Q5NGV7; -.
DR   SMR; Q5NGV7; -.
DR   IntAct; Q5NGV7; 23.
DR   STRING; 177416.FTT_0721c; -.
DR   PeroxiBase; 2678; FtCP01_SCHU.
DR   DNASU; 3192098; -.
DR   EnsemblBacteria; CAG45354; CAG45354; FTT_0721c.
DR   KEGG; ftu:FTT_0721c; -.
DR   eggNOG; COG0376; Bacteria.
DR   OMA; EEIFWGP; -.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   HAMAP; MF_01961; Catal_peroxid; 1.
DR   InterPro; IPR000763; Catalase_peroxidase.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR019794; Peroxidases_AS.
DR   InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR   PANTHER; PTHR30555; PTHR30555; 1.
DR   Pfam; PF00141; peroxidase; 2.
DR   PRINTS; PR00460; BPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Periplasm; Peroxidase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961,
FT                   ECO:0000269|PubMed:16790773"
FT   CHAIN           24..741
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354794"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         264
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   SITE            99
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        102..223
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   249)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        223..249
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   102)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   741 AA;  82501 MW;  51F0EDA67FBB77D4 CRC64;
     MLKKIVTALG MSGMLLASSN AIAEDTTTKN DNLSPQSVDL SPLRNLNKLD SPMDKDYNYH
     QAFKKLDTEQ LKKDMQDLLT QSQDWWPADF GNYGPFFIRL SWHDAGTYRI YDGRGGANRG
     QQRFSPLNSW PDNVNLDKAR QLLWPIKQKY GDAVSWSDLI VLAGTVSLES MGMKPIGFAF
     GREDDWQGDD TNWGLSPEEI MSSNVRDGKL APAYAATQMG LIYVNPEGPD GKPDIKGAAS
     EIRQAFRAMG MTDKETVALI AGGHTFGKTH GAVPEDKVKQ AIGPAPDKAP IEQQGLGWHN
     SYGTGNGDDT MGSGLEGSWT STPTFWNHDF LHNLYNLDWK KTLSPAGAHQ WTPTNAKPEN
     MVPDAHKPGV KHKPIMFTTD LALKEDDGFN KYTQEFYNNP EEFKEEFAKA WFKLTHRDMG
     PKSRYIGPWI PEQNFIWQDP VPAADYKQVS TQDIAQLEQD IINSGLTNQQ LIKTAWDSAS
     TYRKTDYRGG SNGARIALAP EKDWQMNEPA KLEVVLTKLK EIQTNFNNSK TDGTKVSLAD
     LIVLGGNVGV EQAAKQAGYN IQMPFVPGRT DATQAQTDIE SFNYLKTKSD GFINYTDGSV
     SADKLPQTLV EKASMLDLNI PEMTVLVGGM RALDVNYDNS QEGVLTTTPG QLNNSFFVNL
     LDMSTQWKKS DKKDGEYIGI DRKTGKQKWT ASPVDLIFGS NSELKAVAQV YAENGNEQKF
     VNDFAKAWHK VMMLGRFDVQ Q