ID KATG_SYMTH Reviewed; 725 AA. AC Q67LP5; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 120. 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=STH2416; OS Symbiobacterium thermophilum (strain DSM 24528 / JCM 14929 / IAM 14863 / OS T). OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; OC Symbiobacteriaceae; Symbiobacterium. OX NCBI_TaxID=292459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 24528 / JCM 14929 / IAM 14863 / T; RX PubMed=15383646; DOI=10.1093/nar/gkh830; RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., RA Ikeda H., Hattori M., Beppu T.; RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium RT that depends on microbial commensalism."; RL Nucleic Acids Res. 32:4937-4944(2004). 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; AP006840; BAD41401.1; -; Genomic_DNA. DR RefSeq; WP_011196539.1; NC_006177.1. DR AlphaFoldDB; Q67LP5; -. DR SMR; Q67LP5; -. DR STRING; 292459.STH2416; -. DR PeroxiBase; 2350; SthCP01_IAM14863. DR KEGG; sth:STH2416; -. DR eggNOG; COG0376; Bacteria. DR HOGENOM; CLU_025424_2_0_9; -. DR OrthoDB; 9759743at2; -. DR Proteomes; UP000000417; 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:UniProtKB-ARBA. 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..725 FT /note="Catalase-peroxidase" FT /id="PRO_0000354940" FT ACT_SITE 89 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT BINDING 252 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 85 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT CROSSLNK 88..211 FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M- FT 237)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT CROSSLNK 211..237 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W- FT 88)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" SQ SEQUENCE 725 AA; 81957 MW; 951B04CA6355A898 CRC64; MREEDIRSTA GHGTSNKDWW PNQLNLRILH QHSEKANPMG PDFNYREEFK KLDYWALKED LRKLMTESQD WWPADFGHYG PLIIRMAWHS AGTYRIQDGR GGAESGAQRF APLNSWPDNI NLDKARRLLW PIKQKYGRRI SWADLMILAG NVALESMGLK TIGFAGGRAD VWEPEEDIYW GSEQQWLGRD RFGEEGKLED PLAASEMGLI YVNPEGPGRE PDPLKAAQQI RETFKRMGMN DEETVALIAG GHTFGKTHGA ASPSHLGPEP EAAPIEEMGL GWKNSYGTGK GGDTITSGLE VTWTSSPTKW TSNFLWNLFG YEWELTKSPA GAWQWRPKNG AGEGTVPDAH DPNKRHAPGM LTTDIALRVD PVYEKIARRF LENPDEFAKA FARAWFKLTH RDLGPRSRYL GPEVPEEEFI WQDPLPKRDY DLIDEGDIAE LKKRIQASGM SIREMVMTAW ASASTFRGSD KRGGANGARI RLAPQIGWEV NEPEQLRPVL ETLEGIQQEF NRSQTGRKRV SLADLIVLAG CVGIEQAARN AGFEITVPFT PGRVDATQEQ TDVESFSYLE PVHDGFRNYL KRKFSVPAEH LLIDRANLLT LTAPEMTVLI GGLRVLDCNW GRTKHGVLTD RPGALTNDFF VNLLDMRWKW NATDDENVFE GRDRATGELK WTATRVDLIF GSNAQLRAIA EVYASNDGQE KFVQDFVKAW TKVMNLDRFD LLVKK //