KATG_RALSO
ID KATG_RALSO Reviewed; 724 AA.
AC Q8Y1B4; Q8Y1B5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 105.
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};
GN OrderedLocusNames=RSc0776/RSc0775;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD14477.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD14478.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL646052; CAD14477.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL646052; CAD14478.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q8Y1B4; -.
DR SMR; Q8Y1B4; -.
DR STRING; 267608.RSc0775; -.
DR PeroxiBase; 3065; RsoCP01_GMI1000.
DR EnsemblBacteria; CAD14477; CAD14477; RSc0775.
DR EnsemblBacteria; CAD14478; CAD14478; RSc0776.
DR KEGG; rso:RSc0775; -.
DR KEGG; rso:RSc0776; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_3_0_4; -.
DR Proteomes; UP000001436; Chromosome.
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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..724
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354880"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 256
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 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 92..215
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 241)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 215..241
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 92)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 724 AA; 79362 MW; 859F125FCEBB1DA1 CRC64;
MTTESKCPFK HAAAGGGVSN RDWWPNQLNL KVLHQHSSKS DPMDTDFDYA QAFKRLDLAA
VKQDLLALMT TSQDWWPADF GHYGPLFIRM AWHSAGTYRT GDGRGGAGAG QQRFAPLNSW
PDNANLDKAR RLLWPIKQKY GRNISWADLM ILTGNVALES MGFKTFGFAG GRKDVWEPEE
DVYWGSETTW LGDQRYTGDR DLENPLAAVQ MGLIYVNPEG PNGNPDPIAA ARDIRETFAR
MAMNDEETVA LIAGGHSFGK THGAGPAPTW GPEPEAAGIE EQGLGWSSRF GTGKGTDAIT
SGLEVTWTTT PTQWSNNFFQ NLFGYEWELT KSPAGAHQWV AKDAAETIPD AHDPSAKHLP
TMLTTDLSLR FDPAYEKISR RFYEHPEQFA DAFARAWFKL THRDMGPRAR YLGPEVPAEA
LIWQDPIPAV DHKLIDTQDI AALKARILAS GLSVSQLVST AWASASTFRG SDMRGGANGA
RIRLAPQKDW EANQPAQLAK VLETLESIQG AFNGAQSGGK KVSLADLIVL AGCAGVEQAA
KNAGHAVEVP FTPGRMDAAQ AQTDVESFAV LEPIADGFRN YQKGKYTLPA EALLVDKAQL
LTLTAPEMTV LVGGLRVLDT NIGQTRHGVF TQRPESLTND FFVNLLDMGT EWKATDGRDV
FEGRDRATGA LKWTGTRVDL VFGSHSQLRA LAEVYGSADA QAKFVRDFVA AWDKVMNLDR
FDLA
