ID KATG_PSYIN Reviewed; 724 AA. AC A1SWM1; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 04-NOV-2026, entry version 101. 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=Ping_2142; OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Psychromonadaceae; Psychromonas. OX NCBI_TaxID=357804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17664 / CCUG 51855 / 37; RX PubMed=18460197; DOI=10.1186/1471-2164-9-210; RA Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J., RA Land M.L., Thompson L.S.; RT "Genomics of an extreme psychrophile, Psychromonas ingrahamii."; RL BMC Genomics 9:210-210(2008). 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 = 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; CP000510; ABM03886.1; -; Genomic_DNA. DR RefSeq; WP_011770446.1; NC_008709.1. DR AlphaFoldDB; A1SWM1; -. DR SMR; A1SWM1; -. DR STRING; 357804.Ping_2142; -. DR KEGG; pin:Ping_2142; -. DR eggNOG; COG0376; Bacteria. DR HOGENOM; CLU_025424_2_0_6; -. DR OMA; AAKMDFT; -. DR OrthoDB; 9759743at2; -. DR Proteomes; UP000000639; 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 NCBIfam; TIGR00198; cat_per_HPI; 1. DR NCBIfam; NF011635; PRK15061.1; 1. DR PANTHER; PTHR30555:SF6; 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; 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..724 FT /note="Catalase-peroxidase" FT /id="PRO_0000354874" FT ACT_SITE 99 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT BINDING 267 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 95 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT CROSSLNK 98..226 FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M- FT 252)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT CROSSLNK 226..252 FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W- FT 98)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" SQ SEQUENCE 724 AA; 80790 MW; 174148C66597A827 CRC64; MSKNATNTGG KCPVMHGGAT EVSISNMEWW PKALNLDILH QHDSKTNPMG PDFNYREMVK KLDVAALKKD MHALMTESQD WWLADWGHYG GLMIRLSWHA AGTYRIADGR GGAGTGNQRF APINSWPDNV NLDKARRLLW PIKKKYGNKL SWADLIAYAG TIAYESMGLK TFGFAFGRED IWHPEKDTYW GSEKEWLAPS GSEGSRYSGE RDLENPLAAV MMGLIYVNPE GVDGNPDPLK TAHDIRVTFE RMAMNDEETV ALTAGGHTVG KCHGNGDADQ LGAEPEGAEI EDQGFGWLNK TKRGIGRDTV SSGIEGAWTT NPTQWDNGYF QLLLNYEWEL KKSPAGAWQW EPINIKEEHR PVDVEDASIR LTPIMTDADM AMKMDPEYRK ISDRFHQDQD YFSEVFARAW FKLTHRDMGP KVRYIGPDVP QEEQIWQDPV PAGSTDYDIQ AVKDKIAASD LSVSEMVSTA WDSARTFRGS DKRGGANGAR IRLAPQKDWK GNEPARLSKV LAVLEGIAAG SKASVADVIV LAGNVGIEQA AKAAGFDLTV PFSSGRGDAT DEMTDLDSFD VLEPIHDGYR NWLKQDYAVS AEELMLDRTQ LMGLTAHEMT VLIGGMRVIG TNQGGTKHGV LTEHEGTLSN DFFVNLTDMN YTWKPTGNNL YEIRDRKTDK VKWTATRVDL VFGSNSILRA YAEVYAQDDN KEKFVQDFVS AWTKVMNADR FDLI //