KATG_PELPD
ID KATG_PELPD Reviewed; 736 AA.
AC A1ANT3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Ppro_1387;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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; CP000482; ABK99003.1; -; Genomic_DNA.
DR RefSeq; WP_011735296.1; NC_008609.1.
DR AlphaFoldDB; A1ANT3; -.
DR SMR; A1ANT3; -.
DR STRING; 338966.Ppro_1387; -.
DR PeroxiBase; 2348; PprCP01.
DR EnsemblBacteria; ABK99003; ABK99003; Ppro_1387.
DR KEGG; ppd:Ppro_1387; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_7; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000006732; 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..736
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354856"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 265
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 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 96..224
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 250)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 224..250
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 736 AA; 81278 MW; E1CEAA4213E0EE13 CRC64;
MSNDCTCPVT GRVDKPIASS GRANRDWWPH QLNLKILHQN PPLGNPMGEE FSYAEEFKKL
DLEALKKDLY ALMTDSQEWW PADYGHYGGL FIRMAWHSAG TYRTGDGRGG GGSGSQRFAP
LNSWPDNVNL DKARRLLWPI KQKYGRKISW ADLMILAGNC ALESMGFKTF GFGGGREDIW
EPEEDIYWGS EAEWLATSDK PKSRYSGDRD LENPLAAVQM GLIYVNPEGP DGNPDPVASG
RDVRETFGRM AMNDEETVAL VAGGHTFGKC HGAGPATHVG PEPEAAPIEE QGLGWKSSFR
SGKGGDTIGS GIEGAWKPNP TTWDMGYLKV LFKYEWELVK SPAGANQWLA KDVDEEDMVV
DAHDPSKKHR PMMTTADLSL RFDPIYEPIA RDYQQNPEKF ADAFARAWFK LTHRDMGPRS
RYLGAEVPAE ELIWQDPVPT VDHQLIDGQD IAALKDTILA SGLSVSQLVS TAWASASTFR
GSDKRGGANG GRIRLAPQKD WEVNQPAQLK TVLQTLERIQ KEYNDAQSGG KRVSLADLIV
LGGCAGIEQA AKNAGQAVSV PFTPGRTDAT QEQTDVASFA VLEPAADGFR NYLKTRYTVS
AEELLVDRAQ LLTLTAPEMT VLLGGMRVLN ANYGQSRHGV FTKRPETLTN DFFLNLLDMG
TVWKATSEAG DLFEGRDHTS GELKWTATRV DLIFGSNSQL RALAEVYGSG DSQEKFLHDF
VAVWEKVMNL DRFDLA
