KATG_PSEPW
ID KATG_PSEPW Reviewed; 752 AA.
AC B1J7Q1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=PputW619_2235;
OS Pseudomonas putida (strain W619).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=390235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W619;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA Richardson P.;
RT "Complete sequence of Pseudomonas putida W619.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000949; ACA72735.1; -; Genomic_DNA.
DR RefSeq; WP_012314124.1; NC_010501.1.
DR AlphaFoldDB; B1J7Q1; -.
DR SMR; B1J7Q1; -.
DR STRING; 390235.PputW619_2235; -.
DR EnsemblBacteria; ACA72735; ACA72735; PputW619_2235.
DR KEGG; ppw:PputW619_2235; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
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.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..752
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354869"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Basic and acidic residues"
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 752 AA; 82105 MW; 84F29A6453CE4D30 CRC64;
MSNESKCPFH QTAGGGTTNR DWWPDQLNLR ILHQHGTKSD PMDPDFDYAK AFKSLDFQAL
KQDLTALMTD SQDWWPADFG HYGPLFIRMA WHSAGTYRIG DGRGGAGSGQ QRFAPLNSWP
DNVSLDKARR LLWPIKQKYG NKISWADLIV LTGNVALESM GFKTFGFSGG RADVWEPDED
VYWGSEKVWL GGDTRYGKDQ VKAQAPGQGD LVAEPAKHGE EQNRDLSAER NLENPLAAVQ
MGLIYVNPEG PEGNPDPVAS GKDIRETFGR MAMNDEETVA LIAGGHAFGK THGAGPADNV
GAEPEAAGLE LQGLGWANKF GTGKGGDTIT SGLEVTWTST PTQWSNEYLN NLFNFEWELT
KSPAGAHQWQ PKEGKGAGTV PDAHDPSKRH APSMLTSDLA LRFDPIYEPI ARRFKDNPDQ
LADAFARAWY KLIHRDMGPL ARYLGPEMPN EELLWQDPLP KADQPLPSEQ DIAALKTKVL
ASGLSVGELV STAWAAASTF RGSDKRGGAN GARLRLAPQK DWPANQGTGK VLAALEQIQG
EFNNGGKHIS LADLIVLAGT AAVEKAAKDA GYAGNVQFRP GRVDASQEQT DVESFAVLEP
LADGFRNFTK ARYSVKAEKL LLDKAQLLTL TAPELTVLIG GLRVLGANHG GSKHGVFTDQ
PGTLSNDFFR NLLDMGVEWK ATSGDNESFE GRDRKTGQVK WTGTRVDLVF GSHAQLRALS
EVYGSSDGKD KFVKDFVAAW VKVMELDRFD LK
