ID KATG_RHOE4 Reviewed; 740 AA. AC C0ZSW0; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 02-SEP-2026, entry version 84. 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=RER_12250; OS Rhodococcus erythropolis (strain PR4 / NBRC 100887). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Nocardiaceae; Rhodococcus; Rhodococcus erythropolis group. OX NCBI_TaxID=234621; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR4 / NBRC 100887; RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.; RT "Comparison of the complete genome sequences of Rhodococcus erythropolis RT PR4 and Rhodococcus opacus B4."; RL Submitted (MAR-2005) 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=H2O2 + AH2 = 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 = O2 + 2 H2O; 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; Evidence={ECO:0000255|HAMAP- CC 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 --------------------------------------------------------------------------- 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; AP008957; BAH31933.1; -; Genomic_DNA. DR RefSeq; WP_020906506.1; NC_012490.1. DR AlphaFoldDB; C0ZSW0; -. DR SMR; C0ZSW0; -. DR KEGG; rer:RER_12250; -. DR PATRIC; fig|234621.6.peg.1689; -. DR eggNOG; COG0376; Bacteria. DR HOGENOM; CLU_025424_2_0_11; -. DR Proteomes; UP000002204; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA. DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:TreeGrafter. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter. DR CDD; cd00649; catalase_peroxidase_1; 1. DR CDD; cd08200; catalase_peroxidase_2; 1. DR FunFam; 1.10.420.10:FF:000002; Catalase-peroxidase; 1. DR FunFam; 1.10.420.10:FF:000004; Catalase-peroxidase; 1. DR FunFam; 1.10.520.10:FF:000002; Catalase-peroxidase; 1. DR Gene3D; 1.10.520.10; -; 2. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 2. 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 NCBIfam; TIGR00198; cat_per_HPI; 1. DR NCBIfam; NF011635; PRK15061.1; 1. DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1. DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1. DR Pfam; PF00141; peroxidase; 2. DR PRINTS; PR00460; BPEROXIDASE. DR PRINTS; PR00458; PEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 2. 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..740 FT /note="Catalase-peroxidase" FT /id="PRO_1000216226" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 110 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT BINDING 272 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 106 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT CROSSLNK 109..231 FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M- FT 257)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT CROSSLNK 231..257 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W- FT 109)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" SQ SEQUENCE 740 AA; 80838 MW; 89718B33D8DBE547 CRC64; MSDSCPVAHD GNTASTSESE NPAIPSPTPT GNRPRTNRDW WPNQPDLSVL HAHSSKSNPM GADFDYAQEF AKLDVEALKR DVIALMTASQ DWWPADYGHY GGLFVRMSWH AAGTYRIADG RGGGGQGAQR FAPLNSWPDN ASLDKARRLL WPVKQKYGKQ VSWADLLVFA GNCALESMGF TTFGFGFGRE DIWEPEEIYW GPEDTWLGDE RYSGDRELSG PLGAVQMGLI YVNPEGPNGQ PDPVAAARDI RETFARMAMN DVETAALIAG GHTFGKTHGA GPADLVGPEP EGAPVEQQGL GWKSAFGTGV GKDAITSGLE VVWTPTPTKW DNTFLEILYG YDWELTKSPA GAWQWIPKDG AGAGTIPDPF DSSAGRTPTM LTTDLSLRLD PTYEKITRRW LDHPEEFAEE FAKAWYKLLH RDMGPVTRYL GPWVPEPQLW QDPVPSADDQ LIGDADIAIL KSRLLDSGLS VSQLVSTAWA SAASFRSTDM RGGANGARIR LEPQKNWEVN EPATLSAVLQ TLERVQQEFN QAGGAKVSLA DLIVLGGTAA VEQAAKNAGQ DITVSFTPGR TDATQEQTDV DSFEVLEPRA DGFRNYLKGG EKIPAEILLV DRAYMLSLTP PEVTVLVGGL RALNANFGKT GHGVFTDRPE TLTNDFFVNL LDMGTEWKPS KTEENVYDGV DRATGDPKYT ATAVDLVFGS NSQLRALSEV YASEDAKQKF AEDFAAAWTK VMDLDRFDVN //