KATG_PSEPF
ID KATG_PSEPF Reviewed; 755 AA.
AC Q3KE62;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
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}; OrderedLocusNames=Pfl01_2201;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
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}.
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DR EMBL; CP000094; ABA73944.1; -; Genomic_DNA.
DR RefSeq; WP_011333629.1; NC_007492.2.
DR AlphaFoldDB; Q3KE62; -.
DR SMR; Q3KE62; -.
DR STRING; 205922.Pfl01_2201; -.
DR PeroxiBase; 2315; PfCP01_PfO1.
DR World-2DPAGE; 0008:Q3KE62; -.
DR PRIDE; Q3KE62; -.
DR EnsemblBacteria; ABA73944; ABA73944; Pfl01_2201.
DR KEGG; pfo:Pfl01_2201; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000002704; 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.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..755
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354864"
FT REGION 193..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 286
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..245
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 271)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 245..271
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 755 AA; 82734 MW; 33E6BD851C288542 CRC64;
MANESKCPFN HAAGGGTTNR DWWPNQLNLK ILSQHSPASD PMGKDFDYAK AFKSLDFQAL
KRDLTALMTD SQEWWPADFG HYGPLFIRMA WHSAGTYRTA DGRGGAGSGQ QRFAPLNSWP
DNVSLDKARR LLWPIKQKYG RNISWADLIV LTGNVALESM GFKTFGFSGG RADVWEPDED
VYWGSENKWL GGDNRYGKDP ESMQPPGEGT LVAEPAEHGN EESRTNQGER NLENPLAAVQ
MGLIYVNPEG PEGNPDPVAS AKDIRETFGR MAMNDEETVA LIAGGHAFGK THGAGPADNV
GPEPEAAGLE EQGLGWKNSF GTGKGADTIT SGLEVTWTTT PTKWSNNYLE NLFGFEWELT
KSPAGAHQWK PKNGAGAGTI PHAHDPNKRI DPTMLTSDLA LRFDPTYEKI SRRFLANPDQ
LADAFARAWY KLIHRDMGPL SRYLGPELPQ EELLWQDPIP EATHPLVDDS DIRALKGKIL
ASGLSVSELV STAWAAASTF RGSDKRGGAN GGRLRLAPQK FWQANQPEQL DKVLKVLEGI
QNEFNAGAAG KQVSLADLIV LAGNAGVEQA AQNAGHTVTV PFNPGRTDAT QEQTDVESFG
FLEPHTDGFR NYAASTYRVP AEALLIDKAQ LLTLSAPEMT VLIGGLRVLD TNVGKTQHGV
FTDRPGTLTN DFFRNLLDMG VEWKPTSKTE FEGRDRKTGS VKWTATRVDL VFGSNSVLRA
LAEVYASSDA KEQFVTDFVA AWAKVMDLDR FDLRQ
