ID KATG_MARMS Reviewed; 737 AA. AC A6VVN4; DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 25-MAY-2022, entry version 79. 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=Mmwyl1_1585; OS Marinomonas sp. (strain MWYL1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Oceanospirillaceae; Marinomonas. OX NCBI_TaxID=400668; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MWYL1; 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., Bruce D., Detter J.C., Han C., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., RA Richardson P.; RT "Complete sequence of Marinomonas sp. MWYL1."; RL Submitted (JUN-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}. 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; CP000749; ABR70513.1; -; Genomic_DNA. DR AlphaFoldDB; A6VVN4; -. DR SMR; A6VVN4; -. DR STRING; 400668.Mmwyl1_1585; -. DR PeroxiBase; 7192; MAspCP01. DR EnsemblBacteria; ABR70513; ABR70513; Mmwyl1_1585. DR KEGG; mmw:Mmwyl1_1585; -. DR eggNOG; COG0376; Bacteria. DR HOGENOM; CLU_025424_2_0_6; -. DR OMA; MILAGNC; -. 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. FT CHAIN 1..737 FT /note="Catalase-peroxidase" FT /id="PRO_0000354829" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..32 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 104 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT METAL 267 FT /note="Iron (heme b axial ligand)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT SITE 100 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" FT CROSSLNK 103..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 103)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961" SQ SEQUENCE 737 AA; 81182 MW; C16560A20E762F15 CRC64; MSKENMSNEG KCPFNHGAAG TNQSSGRGTS NKDWWPNQLN LNILHQHSPK SNPMGEDFDY AKEFNSLDLE AIRQDLFALM TDSQDWWPAD YGHYGPFFIR MAWHSAGTYR TADGRGGATS GTQRFAPLNS WPDNVNLDKA RRLLWPIKQK YGRKISWADL MILAGNCALE SMGFKTFGFA GGRVDVWQPE EDIYWGTEKT WLDDERYTGD RELENPLAAV QMGLIYVNPE GPEGKPDTLA SARDIRDTFG RMAMNDEETV ALIAGGHTFG KAHGAGDAAQ VGADPEAAGI AEQGFGWSNS MGTGKGVDTI SSGLEGAWTK SPIAWDNGYF ENLFEYDWEL TKSPAGAWQW TPKDGAAANS VPDAHDSSKR HAPIMFTSDL ALRDDPIYAP ISKRFYENPD QLADAFARAW FKLTHRDMGP VARYLGPLVP QEELVWQDPI PAVTYVTVND QDILDLKAKI QASGLTVAQL VSTAWASAST YRGSDMRGGA NGARIRLAPQ KDWAVNQPEQ LAKVLSVLES IQAEFNRQDS TKQVSLADLI VLGGSVGVEQ AAKASGHSVT VPFTAGRADA SQEQTDVESF AFLEPAADGF RNYLKGKYTV SAEEMLVDRA QLLTLSAPEM TALLGGLRVL NANVGQSQHG VFTDKPETLS NDFFVNLLDM GTKWFATSEE EEEFQGRDRT TGKIKWTATR ADLVFGSNSQ LRAIAEVYAC SDSQERFVKD FIAAWTKVME LDRFDLA //