ID   KATG_STRRE              Reviewed;         740 AA.
AC   O87864;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
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};
GN   Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=cpeB;
OS   Streptomyces reticuli.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   SUBUNIT, AND HEME-BINDING.
RC   STRAIN=Tu45;
RX   PubMed=10217488; DOI=10.1099/13500872-145-3-549;
RA   Zou P., Borovok I., Ortiz de Orue Lucana D., Muller D., Schrempf H.;
RT   "The mycelium-associated Streptomyces reticuli catalase-peroxidase, its
RT   gene and regulation by FurS.";
RL   Microbiology 145:549-559(1999).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961,
CC       ECO:0000269|PubMed:10217488}.
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       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10217488}.
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; Y14317; CAA74698.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87864; -.
DR   SMR; O87864; -.
DR   PeroxiBase; 2330; SretCP01.
DR   KEGG; srw:TUE45_00516; -.
DR   OrthoDB; 49441at2; -.
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; Peroxidase.
FT   CHAIN           1..740
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000055577"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        109
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         272
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            105
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        108..231
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   257)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        231..257
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   108)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   740 AA;  81346 MW;  E21860AFE4B4A40E CRC64;
     MTENHDAIVT DAKSEGSGGC PVAHDRALHP TQGGGNRQWW PERLNLKILA KNPAVANPLD
     EDFDYAEAFK ALDLAAVKRD IAEVLTTSQD WWPADFGNYG PLMIRMAWHS AGTYRISDGR
     GGAGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQSI SWADLLILTG NVALETMGFK
     TFGFGGGRAD VWEAEEDVYW GPETTWLDDR RYTGDRELEN PLGAVQMGLI YVNPEGPNGN
     PDPIAAARDI RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADHVGADP EAASLEEQGL
     GWRSTYGTGK GADAITSGLE VTWTSTPTQW SNGFFKNLFE YEYELEQSPA GAHQWVAKNA
     PEIIPDAHDP SKKHRPRMLT TDLSLRFDPI YEPISRRFYE NPEEFADAFA RAWYKLTHRD
     MGPKSLYLGP EVPEETLLWQ DPLPEREGEL IDDADIAILK TKLLESGLSV SQLVTTAWAS
     ASTFRASDKR GGANGARIRL APQRGWEVND PDQLAQVLRT LENVQQEFNA SSGAKKVSLA
     DLIVLGGAAG VEKAAKEAGF EIQVPFTPGR VDATEEHTDV ESFEALEPTA DGFRNYLGKG
     NRLPAEYLLL DKANLLNLSA PEMTVLVGGL RVLGANHQQS QLGVFTKTPG VLTNDFFVNL
     LDMGTTWKAT SEDQTTFEGR DAATGEVKWA GSRADLVFGS NSELRALAEV YASDDAKEKF
     VKDFVAAWHK VMDADRFDLV