KATG_PSEMY
ID KATG_PSEMY Reviewed; 716 AA.
AC A4XZ62;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Pmen_3881;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP86628.1; -; Genomic_DNA.
DR RefSeq; WP_012019778.1; NC_009439.1.
DR AlphaFoldDB; A4XZ62; -.
DR SMR; A4XZ62; -.
DR STRING; 399739.Pmen_3881; -.
DR PRIDE; A4XZ62; -.
DR EnsemblBacteria; ABP86628; ABP86628; Pmen_3881.
DR KEGG; pmy:Pmen_3881; -.
DR PATRIC; fig|399739.8.peg.3934; -.
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 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..716
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354865"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 257
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..216
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 242)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 216..242
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 716 AA; 78341 MW; BCDF2396F57541CB CRC64;
MSNQGKCPFN HVAGGGTTNK DWWPNQLRVD LLNQHSDRSN PLGEKFNYAE AFKKLDYKAL
KADLVRLMTD SQDWWPADFG HYGPQFIRMA WHSAGTYRTT DGRGGGGRGQ QRFAPLNSWP
DNVNIDKSRR LLWPIKQKYG QSISWADLYI LAGNVALESM GFRTFGFGAG REDVWEPDQD
VNWGAEVAWL GVDPKRVNDE RELTAPFGAT HMGLIYVNPE GPNASGDYLA AAKDIRATFY
RMAMNDEEIV ALIAGGHTFG KAHGAAPESH KGPEPEGAPI EAQGLGWTSN FGSGFGKDTV
SSGLEVTWTK TPALWSNNFF ENLFKFEWEL TKSPAGAKQW VAKDAPEIIP DAHVPGKFHK
PTMLTTDLTL RFDPEFGKIS KRFYEDPQAF ADAFARAWYK LTHRDMGPKA RYLGPEVPKE
DLIWQDPLPA AIHNPSAADI ADLKARIAAS GLSVGDLVSV AWASASTFRG GDKRGGANGA
RLALAPQKDW EANQRAIKVL PKLVEIQQAS GKASLADVIV LAGNVGVEQA AKAAGVAVDV
PFAAGRVDAR QDQTDVESFD VLESAADGFR NYSKGNLGVP TETMLVDKAQ LLTLTAPELT
ALVGGLRVLG ANYDGSQHGV FTDKVGVLSN DFFVNLLDMN TVWKAVDDSN EVFEGRGRKD
GQVKYTATRN DLVFGSNSIL RAYAEVYASS DGKEKLVKDF VAAWTKVMNL DRFDLA
