ID   KATG_RHIRD              Reviewed;         723 AA.
AC   Q9R708;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=katA;
OS   Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS   radiobacter).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=A348;
RX   PubMed=10652101; DOI=10.1046/j.1365-2958.2000.01709.x;
RA   Xu X.Q., Pan S.Q.;
RT   "An Agrobacterium catalase is a virulence factor involved in
RT   tumorigenesis.";
RL   Mol. Microbiol. 35:407-414(2000).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity (By similarity). Involved in tumorigenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01961, ECO:0000269|PubMed:10652101}.
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   -!- 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; AB033631; BAA89349.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9R708; -.
DR   SMR; Q9R708; -.
DR   STRING; 1082932.ATCR1_11948; -.
DR   PeroxiBase; 2692; AtuCP01_C58.
DR   eggNOG; COG0376; Bacteria.
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   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; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..723
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354715"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         266
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            94
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        97..225
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   251)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        225..251
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   97)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   723 AA;  78741 MW;  AA531987F535B508 CRC64;
     MDATSKPAGK CPVMHGGNTV SGKSVTEWWP NALNLDILHQ HDTKTNPLGT SFNYREALKT
     LDVEALKADL RALMTDSQEW WPADWGSYVG MMARVTWHAA GSYRVTDGRG GANTGNQRFA
     PLNSWPDNVN TDKGRRLLWP IKKKYGNKIS WADLIALAGT IAYDVAGLKT FGFAFGREDI
     WAPEKDTYWG DEKEWLAPSD GRYGDVSKPE TLENPLAAVQ MGLIYVNPEG VNGKSDPLAT
     AAQMRETFAR MGMDDEETVA LTAGGHTIGK SHGNGSAANL SPDPEAAGPE YQGLGWINTK
     GRGIGRDTVV SGIEGAWTSE PTKWDNGFFD MLFKHEWTLT HSPAGASQWA PITIAEEDKP
     VDVEDASIRT IPMMTDADMA LKVDPIYREI SLKFKDDQDH FSDVFARAWF KLTHRDMGPK
     SRYVGPDVPA EDLIWQDPIP AGSTSYDVAA VKAKIAASGL SVADLVSTAW DSARTFRGSD
     KRGGANGARI RLAPQKDWEG NEPARLSRVL SVLEPIARET GASIADVIVL AGNYGVEQAA
     KAAGFDIAVP FAAGRGDASA EQTDADSFAP LEPLADGFRN WVKKDYVVSP EELLLDRAQL
     LGLTAPELTV LIGGLRVIGA NYGGAAHGVF TDKPGALTTD FFTTLTDMAY SWVPTGNNLY
     EIRDRKTGAA RYSATRVDLV IGSNSILRAY AEVYAQDDNR EKFARDFIAA WTKVMNADRF
     DLI